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1KOL

Crystal structure of formaldehyde dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0018467molecular_functionformaldehyde dehydrogenase activity
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
A0046872molecular_functionmetal ion binding
A0047895molecular_functionformaldehyde dismutase activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0018467molecular_functionformaldehyde dehydrogenase activity
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0046872molecular_functionmetal ion binding
B0047895molecular_functionformaldehyde dismutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS46
AHIS67
AASP169
ANAD1403
AHOH1404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
ACYS97
ACYS100
ACYS103
ACYS111

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 1003
ChainResidue
BCYS46
BHIS67
BASP169
BNAD2403
BHOH2404

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1004
ChainResidue
BCYS97
BCYS100
BCYS103
BCYS111

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
APRO241
ALEU242
AHIS269
AHOH1548
AHOH1618
AHOH1634
AHOH1735
AHOH1836

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BPRO241
BLEU242
BHIS269
BHOH2656
BHOH2667
BHOH2718
BHOH2846

site_idAC7
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAD A 1403
ChainResidue
AGLY47
ASER48
AGLN50
AHIS51
APHE93
AASP169
ATHR173
AGLY193
AGLY195
APRO196
AVAL197
AGLY216
AASP217
ALEU218
AARG222
AALA261
AVAL262
AALA266
AARG267
AHIS269
AVAL282
APRO299
ALEU301
ATRP327
AGLY336
AGLN337
ATHR338
APHE379
AZN1001
AHOH1409
AHOH1415
AHOH1426
AHOH1450
AHOH1467
AHOH1579

site_idAC8
Number of Residues40
DetailsBINDING SITE FOR RESIDUE NAD B 2403
ChainResidue
BHOH2422
BHOH2425
BHOH2427
BHOH2482
BHOH2490
BHOH2503
BHOH2602
BHOH2670
BHOH2691
BGLY47
BSER48
BGLN50
BHIS51
BPHE93
BASP169
BTHR173
BGLY193
BGLY195
BPRO196
BVAL197
BGLY216
BASP217
BLEU218
BARG222
BLEU236
BALA261
BVAL262
BALA266
BARG267
BHIS269
BVAL282
BPRO299
BLEU301
BTRP327
BGLY336
BGLN337
BTHR338
BPHE379
BZN1003
BHOH2404

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiTGEviekGrdV
ChainResidueDetails
AGLY66-VAL80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:12445786, ECO:0007744|PDB:1KOL
ChainResidueDetails
AGLY47
ALEU112
AGLY198
ALEU218
ALEU223
AGLY263
AGLY268
AGLY300
AGLN337
BGLY47
BSER48
BGLU68
BGLY98
BARG101
BLYS104
BLEU112
BGLY198
BLEU218
BLEU223
BGLY263
BGLY268
BGLY300
BGLN337
ASER48
AGLU68
AGLY98
AARG101
ALYS104

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1KOL
ChainResidueDetails
AILE170
BILE170

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PDB entries from 2024-04-17

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