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1VNS

RECOMBINANT APO-CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0016691molecular_functionchloride peroxidase activity
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 610
ChainResidue
ALYS353
AARG360
APHE397
ASER402
AGLY403
AHIS404
AARG490
AHIS496
AHOH1111

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 611
ChainResidue
AALA95
AASN96
AASP97
ASER156
AALA157
ASER158
AHOH1248

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8552646
ChainResidueDetails
AHIS404

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:8552646, ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ, ECO:0007744|PDB:1VNC
ChainResidueDetails
ALYS353
AARG360
ASER402
AGLY403
AHIS404
AARG490
AHIS496

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1vnc
ChainResidueDetails
ALYS353
AHIS404

site_idMCSA1
Number of Residues7
DetailsM-CSA 14
ChainResidueDetails
ALYS353electrostatic stabiliser, hydrogen bond donor
AARG360electrostatic stabiliser, hydrogen bond donor
ASER402electrostatic stabiliser, hydrogen bond donor
AGLY403electrostatic stabiliser, hydrogen bond donor
AHIS404activator, hydrogen bond acceptor
AARG490electrostatic stabiliser, hydrogen bond donor
AHIS496covalently attached, metal ligand

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PDB entries from 2024-07-10

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