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4YZW

Crystal structure of AgPPO8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004097molecular_functioncatechol oxidase activity
A0004497molecular_functionmonooxygenase activity
A0005576cellular_componentextracellular region
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004097molecular_functioncatechol oxidase activity
B0004497molecular_functionmonooxygenase activity
B0005576cellular_componentextracellular region
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CU A 801
ChainResidue
AHIS223
AHIS227
AHIS252

site_idAC2
Number of Residues3
Detailsbinding site for residue CU A 802
ChainResidue
AHIS379
AHIS383
AHIS419

site_idAC3
Number of Residues3
Detailsbinding site for residue CU B 801
ChainResidue
BHIS223
BHIS227
BHIS252

site_idAC4
Number of Residues3
Detailsbinding site for residue CU B 802
ChainResidue
BHIS379
BHIS383
BHIS419

Functional Information from PROSITE/UniProt
site_idPS00210
Number of Residues9
DetailsHEMOCYANIN_2 Arthropod hemocyanins / insect LSPs signature 2. TamRDPiFY
ChainResidueDetails
ATHR408-TYR416

site_idPS00498
Number of Residues12
DetailsTYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPiFYrwHkfiD
ChainResidueDetails
AASP412-ASP423

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsPropeptide: {"featureId":"PRO_0000452495","evidences":[{"source":"UniProtKB","id":"Q8I6K1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"26732497","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26732497","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YZW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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