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2Z98

The crystal structure of AzoR (azoreductase) from Escherichia coli: Oxidized AzoR in tetragonal crystals (The resolution has improved from 1.8 (1v4b) to 1.4 angstrom)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016652molecular_functionoxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0042803molecular_functionprotein homodimerization activity
A0050446molecular_functionazobenzene reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN A 201
ChainResidue
ASER9
AASN97
APHE98
ASER139
AARG140
AGLY141
AGLY142
AHIS144
AHOH233
AHOH258
ALEU11
ASER15
AGLN16
ASER17
ALEU50
APRO94
AMET95
ATYR96

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
APHE98
AASN99
ALEU151
ATYR155

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
APHE170
APHE172
AASP189

Functional Information from SwissProt/UniProt

219869

PDB entries from 2024-05-15

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