Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4C7Z

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), activated with sodium dithionite and sodium sulfide

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 918
ChainResidue
AHOH2208
AHOH2213
AHOH2378
AHOH3233
AHOH3234
AHOH3235

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 920
ChainResidue
AHOH3238
AHOH3239
AHOH3240
AHOH2876
AHOH3236
AHOH3237

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 1908
ChainResidue
AGLN99
ACYS100
AGLY101
ACYS103
ACYS137
AARG138
ACYS139
AILE368

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES A 1909
ChainResidue
AGLY39
ACYS40
AGLU41
AGLY43
AGLN44
ACYS45
AGLY46
ACYS48
ACYS60

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 1910
ChainResidue
AALA531
ATYR535
ALEU626
AGLY697
APEO1916
AHOH2870

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT A 1911
ChainResidue
AARG460
ASER461
ALEU498
AALA531
APHE532
ATYR535
AGLY536
AGLN539
AHOH2845

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1912
ChainResidue
AASP263
AGLU899
AGLU903
AHOH2611
AHOH2612
AHOH3241

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1913
ChainResidue
ALYS248
APRO898
AGLU899
AHOH2564

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1914
ChainResidue
ATYR892
AARG893
AHOH2708

site_idBC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE PCD A 1915
ChainResidue
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
ASER865
AGLY866
AVAL867
AGLY868
AGLU869
APEO1916
AHOH3015
AHOH3052

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEO A 1916
ChainResidue
AALA531
AGLY696
AGLY697
AGLU869
AIPA1910
APCD1915

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
AGLU869covalently attached, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon