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3FC4

Ethylene glycol inhibited form of Aldehyde oxidoreductase from Desulfovibrio gigas

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 919
ChainResidue
AHOH1148
AHOH1620
AHOH1798
AHOH1862
AHOH1944
AHOH2063

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 920
ChainResidue
AHOH1097
ALYS248
APRO898
AGLU899

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 916
ChainResidue
AARG460
ATYR535
AGLN539

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 917
ChainResidue
AASP263
AGLU899
AGLU903
AHOH1379
AHOH1442
AHOH1520

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 918
ChainResidue
ATYR892
AARG893
AHOH1867

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 915
ChainResidue
AHOH927
AHOH928
AHOH929
AHOH1144
AHOH1145
AHOH1183

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 908
ChainResidue
AGLN99
ACYS100
AGLY101
ACYS103
ACYS137
AARG138
ACYS139
AILE368

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES A 909
ChainResidue
AGLY39
ACYS40
AGLU41
AGLY43
AGLN44
ACYS45
AGLY46
ACYS48
ACYS60

site_idAC9
Number of Residues36
DetailsBINDING SITE FOR RESIDUE PCD A 921
ChainResidue
AGLN99
ACYS139
AGLY419
ATHR420
APHE421
AGLY422
AALA531
APHE532
AARG533
ATRP650
AHIS653
AGLY654
AGLN655
AGLY656
AGLY660
ASER695
AGLY696
AGLY697
AARG699
AGLN700
AGLN701
ALEU795
ASER797
ACYS799
AASN800
ATHR804
AGLN807
AALA864
ASER865
AGLY866
AVAL867
AGLY868
AGLU869
AEDO912
AHOH1199
AHOH1361

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 910
ChainResidue
ALYS472
ALYS473
ALYS473
AASP474

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 911
ChainResidue
ALEU254
AILE255
ATHR256
AALA780
ATHR781
ALEU902
AHOH932
AHOH1396
AHOH1729
AHOH1781

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 912
ChainResidue
AGLY696
AGLY697
AGLU869
APCD921
AHOH1335
APHE425
AALA531
ATYR535
ATYR622

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_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
AGLU869

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

226707

PDB entries from 2024-10-30

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