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6JUK

Crystal structure of Formate dehydrogenase mutant C256I/E261P/S381I from Pseudomonas sp. 101 in complex with non-natural cofactor Nicotinamide Cytosine Dinucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008863molecular_functionformate dehydrogenase (NAD+) activity
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
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008863molecular_functionformate dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042183biological_processformate catabolic process
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 501
ChainResidue
AHIS30
AGLY33
AHOH608

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
ATYR9
AASP10
ATRP100
AHOH666
AHOH737
BTRP178

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 503
ChainResidue
ATHR74
ASER75
AHOH724

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
ATYR20
AARG22
AASP23
ATHR46
APRO47
AGLY48
BHOH627

site_idAC5
Number of Residues25
Detailsbinding site for residue A7R A 505
ChainResidue
APHE99
AASN147
AVAL151
AALA199
AGLY201
AARG202
AILE203
AASP222
AARG223
AASN255
AILE256
APRO257
AHIS259
ATHR283
AALA284
AASP309
AHIS333
ASER335
AGLY336
AHOH624
AHOH663
AHOH707
AHOH741
AHOH771
AHOH773

site_idAC6
Number of Residues23
Detailsbinding site for residue A7R B 501
ChainResidue
BPHE99
BASN147
BVAL151
BALA199
BGLY201
BARG202
BILE203
BASP222
BARG223
BASN255
BILE256
BPRO257
BHIS259
BTHR283
BALA284
BASP309
BHIS333
BSER335
BGLY336
BHOH606
BHOH645
BHOH682
BHOH740

site_idAC7
Number of Residues2
Detailsbinding site for residue GOL B 502
ChainResidue
BARG360
BPRO361

site_idAC8
Number of Residues2
Detailsbinding site for residue GOL B 503
ChainResidue
BHIS259
BHOH615

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlrrlapfdvh.LHyTD
ChainResidueDetails
AVAL195-ASP222

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYpvCDVVtLNiPlhppTehMiN
ChainResidueDetails
AMET245-ASN267

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKrGaYIVNtARGkLCD
ChainResidueDetails
APHE274-ASP290

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|DOI:10.1134/S1063774506040146
ChainResidueDetails
AILE123
AASN147
BILE123
BASN147

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:8114093
ChainResidueDetails
ASER148
BARG202
BASP222
BPRO257
BTHR283
BASP309
BHIS333
BILE381
AARG202
AASP222
APRO257
ATHR283
AASP309
AHIS333
AILE381
BSER148

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305|PubMed:8114093
ChainResidueDetails
AARG285
AHIS333
BARG285
BHIS333

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 902
ChainResidueDetails
AASN147electrostatic stabiliser
AARG285electrostatic stabiliser
AGLN314modifies pKa
AHIS333enhance reactivity

site_idMCSA2
Number of Residues4
DetailsM-CSA 902
ChainResidueDetails
BASN147electrostatic stabiliser
BARG285electrostatic stabiliser
BGLN314modifies pKa
BHIS333enhance reactivity

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PDB entries from 2024-04-24

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