5W6P

Crystal structure of Bacteriophage CBA120 tailspike protein 2 enzymatically active domain (TSP2dN, orf211)

External Resource: Annotation

Domain Annotation: ECOD Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e5w6pA2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
A	F_UNCLASSIFIED	e5w6pA3	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
A	F_UNCLASSIFIED	e5w6pA1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e5w6pB2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e5w6pB3	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e5w6pB1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e5w6pC2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e5w6pC3	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e5w6pC1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e5w6pD2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e5w6pD3	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e5w6pD1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
E	F_UNCLASSIFIED	e5w6pE2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
E	F_UNCLASSIFIED	e5w6pE3	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
E	F_UNCLASSIFIED	e5w6pE1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
F	F_UNCLASSIFIED	e5w6pF3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: F_UNCLASSIFIED	ECOD (1.6)
F	F_UNCLASSIFIED	e5w6pF1	A: beta sandwiches	X: tailspike protein Orf211 N-terminal domain (From Topology)	H: tailspike protein Orf211 N-terminal domain (From Topology)	T: tailspike protein Orf211 N-terminal domain	F: F_UNCLASSIFIED	ECOD (1.6)
F	F_UNCLASSIFIED	e5w6pF2	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)

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.