6RKC

Inter-dimeric interface controls function and stability of S-methionine adenosyltransferase from U. urealiticum

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6rkca1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
B	d6rkcb1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
B	d6rkcb4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
C	d6rkcc1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
D	d6rkcd1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
E	d6rkce1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
F	d6rkcf1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
F	d6rkcf4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
G	d6rkcg1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)
H	d6rkch1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Ureaplasma urealyticum serovar 7 str. ATCC 27819 ) [TaxId: 519849 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00438	e6rkcA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
A	PF02772	e6rkcA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
A	PF02773	e6rkcA1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
B	PF00438	e6rkcB2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
B	PF02772	e6rkcB3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
B	PF02773	e6rkcB1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
C	PF00438	e6rkcC1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
C	PF02772	e6rkcC2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
C	PF02773	e6rkcC3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
D	PF00438	e6rkcD2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
D	PF02772	e6rkcD3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
D	PF02773	e6rkcD1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
E	PF00438	e6rkcE1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
E	PF02772	e6rkcE3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
E	PF02773	e6rkcE2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
F	PF00438	e6rkcF1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
F	PF02772	e6rkcF3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
F	PF02773	e6rkcF2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
G	PF00438	e6rkcG2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
G	PF02772	e6rkcG1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
G	PF02773	e6rkcG3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
H	PF00438	e6rkcH2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
H	PF02772	e6rkcH3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
H	PF02773	e6rkcH1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
B	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
C	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
D	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
E	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
F	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
G	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)
H	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (utative)

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.

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6RKC

Inter-dimeric interface controls function and stability of S-methionine adenosyltransferase from U. urealiticum

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: ECOD Classification ECOD Database Homepage

Domain Annotation: CATH CATH Database Homepage