2B3I

NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (19 STRUCTURES)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2b3ia_	All beta proteins	Cupredoxin-like	Cupredoxins	Plastocyanin/azurin-like	Plastocyanin	(Prochlorothrix hollandica ) [TaxId: 1223 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cupredoxins	8034750	3000886	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00127	e2b3iA1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: PF00127	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00127	Copper binding proteins, plastocyanin/azurin family (Copper-bind)	Copper binding proteins, plastocyanin/azurin family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN (PLASTOCYANIN)	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding electron transfer activity	-	intracellular anatomical structure plasma membrane-derived chromatophore membrane membrane plasma membrane plasma membrane-derived chromatophore cellular anatomical entity thylakoid membrane intracellular organelle cell periphery plasma membrane-derived thylakoid membrane organelle intracellular non-membrane-bounded organelle plasma membrane region bacterial thylakoid intracellular anatomical structure plasma membrane-derived chromatophore membrane membrane plasma membrane plasma membrane-derived chromatophore cellular anatomical entity thylakoid membrane intracellular organelle cell periphery plasma membrane-derived thylakoid membrane organelle intracellular non-membrane-bounded organelle plasma membrane region bacterial thylakoid cytoplasm photosynthetic membrane thylakoid non-membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002387	Plastocyanin	Family
A	IPR000923	Blue (type 1) copper domain	Domain
A	IPR028871	Blue (type 1) copper protein, binding site	Binding Site
A	IPR008972	Cupredoxin	Homologous Superfamily
A	IPR023511	Plastocyanin, cyanobacteria	Family
A	IPR001235	Blue (type 1) copper protein, plastocyanin-type	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	plastoquinol-plastocyanin reductase M-CSA #278	Plastocyanin (PC) is a small (approx 10 kDa), type 1 (blue) copper protein that functions as an electron donor to Photosystem I (PSI) from cytochrome (cyt) f in both chloroplast systems and in some strains of cyanobacteria.	Defined by 4 residues: HIS:A-39CYS:A-82HIS:A-85MET:A-90 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.10.99.1 (PDB Primary Data) Search M-CSA Motif + EC 1.10.99.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.