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1OXY

CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0031404molecular_functionchloride ion binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 629
ChainResidue
AHIS324
AHIS328
AHIS364
ACU630
AOXY631

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 630
ChainResidue
AOXY631
AHIS173
AHIS177
AHIS204
ACU629

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXY A 631
ChainResidue
APHE49
AHIS173
AHIS177
AHIS204
AHIS324
AHIS328
APHE360
AHIS364
ACU629
ACU630

Functional Information from PROSITE/UniProt
site_idPS00209
Number of Residues20
DetailsHEMOCYANIN_1 Arthropod hemocyanins / insect LSPs signature 1. YYrEDVgiNahhwhwHlvyP
ChainResidueDetails
ATYR162-PRO181

site_idPS00210
Number of Residues9
DetailsHEMOCYANIN_2 Arthropod hemocyanins / insect LSPs signature 2. TslRDPiFY
ChainResidueDetails
ATHR353-TYR361

site_idPS00498
Number of Residues12
DetailsTYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPiFYnwHrfiD
ChainResidueDetails
AASP357-ASP368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8518732
ChainResidueDetails
AHIS173
AHIS177
AHIS204
AHIS324
AHIS328
AHIS364

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Blocked amino end (Thr); partial => ECO:0000269|PubMed:3525550
ChainResidueDetails
ATHR1

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN449

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
ATYR320

222624

PDB entries from 2024-07-17

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