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2AZA

STRUCTURE OF AZURIN FROM ALCALIGENES DENITRIFICANS. REFINEMENT AT 1.8 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO CRYSTALLOGRAPHICALLY INDEPENDENT MOLECULES

Replaces:  1AZA
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 Residues5
DetailsBINDING SITE FOR RESIDUE CU A 130
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 135
ChainResidue
AALA75
AGLY76
AHIS83
AHOH146
AHOH197

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 136
ChainResidue
ALYS41
ALYS41

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 130
ChainResidue
BGLY45
BHIS46
BCYS112
BHIS117
BMET121

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 135
ChainResidue
BLYS74
BGLY76
BHIS83
BHOH154
BHOH166

site_idM1A
Number of Residues5
Detailsresidues INTERACTING WITH THE COPPER ATOM. THE COPPER FORMS FIVE BONDS
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idM1B
Number of Residues5
Detailsresidues INTERACTING WITH THE COPPER ATOM. THE COPPER FORMS FIVE BONDS
ChainResidue
BMET121
BGLY45
BHIS46
BCYS112
BHIS117

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues17
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GeaYaYFCsfPgHwam.M
ChainResidueDetails
AGLY105-MET121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:3210236
ChainResidueDetails
AHIS46
ACYS112
AHIS117
AMET121
BHIS46
BCYS112
BHIS117
BMET121

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PDB entries from 2024-10-16

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