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4C80

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with hydrogen peroxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0033727molecular_functionaldehyde dehydrogenase (FAD-independent) activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 908
ChainResidue
AGLN99
ACYS100
AGLY101
ACYS103
ACYS137
AARG138
ACYS139
AILE368

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES A 909
ChainResidue
ACYS40
AGLU41
AGLY43
AGLN44
ACYS45
AGLY46
ACYS48
ACYS60
AGLY39

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IPA A 911
ChainResidue
ALYS884
AVAL889
AARG890
ATYR892
AHOH2786

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT A 912
ChainResidue
AARG460
ASER461
ALEU498
AALA531
APHE532
ATYR535
AGLY536
AGLN539
AHOH2734

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A 913
ChainResidue
AGLN29
AHOH2072
AHOH2078
AHOH2383
AHOH2384
AHOH2384
AHOH3092
AHOH3092

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 914
ChainResidue
AGLN214
ALYS216
AGLN452
AHOH2410
AHOH2729
AHOH2730
AHOH2732

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 915
ChainResidue
AASP263
AGLU899
AGLU903
AHOH3074
AHOH3077
AHOH3085

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 916
ChainResidue
AHOH2769
AHOH3093
AHOH3094
AHOH3095
AHOH3096
AHOH3097

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 917
ChainResidue
AHOH2187
AHOH2192
AHOH2326
AHOH3098
AHOH3099
AHOH3100

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 918
ChainResidue
ATYR892
AARG893
AHOH2608

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 919
ChainResidue
ALYS248
APRO898
AGLU899

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 920
ChainResidue
AGLY344

site_idBC4
Number of Residues36
DetailsBINDING SITE FOR RESIDUE PCD A 921
ChainResidue
ASER865
AGLY866
AVAL867
AGLY868
AGLU869
APEO922
AHOH2895
AHOH2924
AGLN99
ACYS139
ATHR420
APHE421
AGLY422
AALA531
APHE532
AARG533
ATRP650
AHIS653
AGLY654
AGLN655
AGLY656
AGLY660
ASER695
AGLY696
AGLY697
ASER698
AARG699
AGLN700
AGLN701
ALEU795
ASER797
ACYS799
AASN800
ATHR804
AGLN807
AALA864

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEO A 922
ChainResidue
AALA531
AGLY696
AGLY697
AGLU869
APCD921
AHOH2864

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CEQGQCGAC
ChainResidueDetails
ACYS40-CYS48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:7502041
ChainResidueDetails
ACYS40
ACYS45
ACYS48
ACYS60
ACYS100
ACYS103
ACYS137
ACYS139

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AHIS653
AGLU869

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 105
ChainResidueDetails
ATHR873covalently attached, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor

238268

PDB entries from 2025-07-02

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