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3JTM

Structure of recombinant formate dehydrogenase from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009579cellular_componentthylakoid
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042183biological_processformate catabolic process
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AARG354
APRO362
AHOH432
AHOH580
AHOH590
AHOH671

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
ALYS45
ATYR184
AARG185

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 4
ChainResidue
ATYR102
ATHR104
ALYS204
ALEU223
AMET225
AALA226
ALEU229
AHOH459
AHOH635

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 5
ChainResidue
AHOH7
AVAL53
AGLU54
AASN55
AALA56
AARG60

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 8
ChainResidue
APRO97
APHE98
AGLY121
AILE122
AASN146
AGLY335
ATYR344
AHOH400
AHOH403
AHOH622
AHOH756

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 9
ChainResidue
ALEU57
AGLY58
ALYS349
AGOL386
AHOH437
AHOH475
AHOH484
AHOH492

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 11
ChainResidue
AASN146
AASN282
AALA283
AHOH440
AHOH622
AHOH717

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE AZI A 379
ChainResidue
AASP360

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 380
ChainResidue
AARG290
APRO312
APRO316
AASP318

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 381
ChainResidue
ATYR187
AASP249

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 382
ChainResidue
AILE108
ALYS109
AALA111
ALYS112
ATHR363
AGLN376
AHOH505
AHOH662
AHOH747

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 383
ChainResidue
AGLY123
ASER124
AASP125
AGLU141
AILE367
ATYR377
AHOH586

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 384
ChainResidue
AGLY200
AARG201
AGOL387

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE AZI A 385
ChainResidue
ALEU161
AASN164
AGLY303
AGLY304
AASN326
AHOH596

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 386
ChainResidue
AGOL9
ALYS349
AHOH435

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 387
ChainResidue
ATHR104
AALA105
AGLU106
AASP128
AGLY200
AASP221
AGOL384
AHOH434
AHOH742

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGTVGaGRIGklllqrlkpfgcn.LLyHD
ChainResidueDetails
AILE194-ASP221

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MLpkCDVIvINmPltekTrgMfN
ChainResidueDetails
AMET244-ASN266

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LKkGvLIVNnARGaIME
ChainResidueDetails
ALEU273-GLU289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210
ChainResidueDetails
AILE122
AASN146

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|Ref.10
ChainResidueDetails
AARG201
AASP221
APRO256
AASN282
AASP308
AHIS332

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210
ChainResidueDetails
AARG284
AHIS332

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PDB entries from 2024-08-14

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