1IDU

CRYSTAL STRUCTURE OF THE PEROXIDE FORM OF THE VANADIUM-CONTAINING CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0016691	molecular_function	chloride peroxidase activity
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE VO4 A 1579

Chain	Residue
A	LYS353
A	HIS496
A	ARG360
A	PRO395
A	PHE397
A	SER402
A	GLY403
A	HIS404
A	ARG490
A	VAL495

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:8552646

Chain	Residue	Details
A	HIS404

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:8552646, ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ, ECO:0007744|PDB:1VNC

Chain	Residue	Details
A	ARG360
A	SER402
A	GLY403
A	HIS404
A	ARG490
A	HIS496
A	LYS353

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 14

Chain	Residue	Details
A	LYS353	electrostatic stabiliser, hydrogen bond donor
A	ARG360	electrostatic stabiliser, hydrogen bond donor
A	SER402	electrostatic stabiliser, hydrogen bond donor
A	GLY403	electrostatic stabiliser, hydrogen bond donor
A	HIS404	activator, hydrogen bond acceptor
A	ARG490	electrostatic stabiliser, hydrogen bond donor
A	HIS496	covalently attached, metal ligand

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