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1ADW

PSEUDOAZURIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 130
ChainResidue
AHIS40
ACYS78
AHIS81
AMET86

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 130
ChainResidue
BMET86
BHIS40
BCYS78
BHIS81

site_idCUA
Number of Residues1
DetailsCU BINDING SITE - HIS 40, CYS 78, HIS 81, AND MET 86 ARE LIGANDS TO THE COPPER.
ChainResidue
ACU130

site_idCUB
Number of Residues1
DetailsCU BINDING SITE - HIS 40, CYS 78, HIS 81, AND MET 86 ARE LIGANDS TO THE COPPER.
ChainResidue
BCU130

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues15
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. Gl.YgVKCt.P.HfgmgM
ChainResidueDetails
AGLY72-MET86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues176
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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