2YL7

CYTOCHROME C PRIME FROM ALCALIGENES XYLOSOXIDANS: AS ISOLATED L16G VARIANT AT 0.9 A RESOLUTION - RESTRAINT REFINEMENT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEC A 128

Chain	Residue
A	ARG12
A	ALA68
A	ILE72
A	GLN83
A	PHE86
A	CYS116
A	CYS119
A	HIS120
A	TYR123
A	ARG124
A	CMO155
A	GLN13
A	HOH2074
A	HOH2327
A	HOH2328
A	HOH2330
A	GLY16
A	MET19
A	ALA20
A	TRP56
A	PHE59
A	GLY65
A	ASP67

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO A 155

Chain	Residue
A	MET19
A	PRO55
A	HEC128
A	HOH2047
A	HOH2330

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:11060017, ECO:0000269|PubMed:11300792, ECO:0007744|PDB:1CGN, ECO:0007744|PDB:1CGO, ECO:0007744|PDB:1E83

Chain	Residue	Details
A	ARG12
A	GLN13
A	ASP67

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: covalent => ECO:0000269|PubMed:11060017, ECO:0000269|PubMed:11300792, ECO:0007744|PDB:1CGN, ECO:0007744|PDB:1CGO, ECO:0007744|PDB:1E83

Chain	Residue	Details
A	CYS116
A	CYS119

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: axial binding residue => ECO:0000269|PubMed:11060017, ECO:0000269|PubMed:11300792, ECO:0007744|PDB:1CGN, ECO:0007744|PDB:1CGO, ECO:0007744|PDB:1E83

Chain	Residue	Details
A	HIS120

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:11060017, ECO:0000269|PubMed:4360249, ECO:0007744|PDB:1E83, ECO:0007744|PDB:1E84, ECO:0007744|PDB:1E86

Chain	Residue	Details
A	PCA1

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