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3WR5

Structural basis on the efficient CO2 reduction of acidophilic formate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide 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
C0000166molecular_functionnucleotide binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008863molecular_functionformate dehydrogenase (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0042183biological_processformate catabolic process
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008863molecular_functionformate dehydrogenase (NAD+) activity
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0042183biological_processformate catabolic process
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
APHE99
AASP222
AARG223
AHIS224
AASN255
AVAL256
APRO257
AHIS259
AGLU261
ATHR262
ATHR283
AILE123
AARG285
AASP309
AVAL310
AHIS333
ASER335
AGLY336
ASER381
AHOH610
AHOH614
AHOH616
AASN147
AHOH620
AHOH629
AHOH682
AHOH915
AHOH916
ASER148
AVAL151
AALA199
AGLY201
AARG202
AILE203

site_idAC2
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAD B 501
ChainResidue
BILE123
BASN147
BSER148
BVAL151
BALA199
BGLY201
BARG202
BILE203
BASP222
BARG223
BHIS224
BASN255
BVAL256
BPRO257
BHIS259
BGLU261
BTHR262
BTHR283
BALA284
BARG285
BASP309
BHIS333
BSER335
BGLY336
BSER381
BHOH609
BHOH610
BHOH613
BHOH664
BHOH666
BHOH705
BHOH753
BHOH808
BHOH810
BHOH884

site_idAC3
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAD C 501
ChainResidue
CHOH658
CHOH666
CHOH672
CHOH692
CILE123
CASN147
CSER148
CVAL151
CALA199
CGLY201
CARG202
CILE203
CASP222
CARG223
CHIS224
CASN255
CVAL256
CPRO257
CHIS259
CGLU261
CTHR262
CTHR283
CALA284
CARG285
CASP309
CVAL310
CHIS333
CSER335
CGLY336
CSER381
CHOH625
CHOH626
CHOH631
CHOH643

Functional Information from PROSITE/UniProt
site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYphCDVVtLNvPlhpeTehMiN
ChainResidueDetails
AMET245-ASN267

221716

PDB entries from 2024-06-26

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