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3JV7

Structure of ADH-A from Rhodococcus ruber

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS92
ACYS95
ACYS98
ACYS106

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS38
AHIS62
AASP153
ANAD503
AACY504

site_idAC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAD A 503
ChainResidue
AHIS39
ASER40
AASP153
ATHR157
AVAL180
AGLY181
AGLY182
ALEU183
AASP203
ALEU204
AARG208
ASER223
APHE246
AVAL247
ATHR252
AVAL269
AGLY270
AILE271
APRO293
ATYR294
ATRP295
ALEU332
AARG340
AHOH346
AHOH351
AHOH368
AHOH369
AHOH371
AHOH412
AHOH414
AHOH418
AHOH422
AZN502
AACY504
DPHE281

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 504
ChainResidue
ACYS38
ASER40
AHIS62
AASP153
ATRP295
AZN502
ANAD503
AMPD505

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 505
ChainResidue
AMET47
ATYR54
ATYR294
AHOH347
AACY504

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS92
BCYS95
BCYS98
BCYS106

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS38
BHIS62
BASP153
BNAD503
BACY504

site_idAC8
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAD B 503
ChainResidue
BHIS39
BSER40
BASP153
BTHR157
BVAL180
BGLY181
BGLY182
BLEU183
BASP203
BLEU204
BARG208
BSER223
BPHE246
BVAL247
BTHR252
BVAL269
BGLY270
BILE271
BPRO293
BTYR294
BTRP295
BARG340
BHOH346
BHOH347
BHOH376
BHOH378
BHOH380
BHOH405
BHOH438
BZN502
BACY504
BHOH620
CPHE281

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 504
ChainResidue
BCYS38
BSER40
BHIS62
BASP153
BTRP295
BZN502
BNAD503
BMPD505

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 505
ChainResidue
BMET47
BTYR54
BHOH469
BACY504

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 501
ChainResidue
CCYS92
CGLY93
CCYS95
CCYS98
CCYS106

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 502
ChainResidue
CCYS38
CHIS62
CASP153
CNAD503
CACY504

site_idBC4
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAD C 503
ChainResidue
BPHE281
CHIS39
CSER40
CASP153
CTHR157
CVAL180
CGLY181
CGLY182
CLEU183
CASP203
CLEU204
CARG208
CSER223
CPHE246
CVAL247
CTHR252
CVAL269
CGLY270
CILE271
CPRO293
CTYR294
CTRP295
CLEU332
CARG340
CHOH354
CHOH359
CHOH363
CHOH364
CHOH372
CHOH377
CZN502
CACY504
CHOH683

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY C 504
ChainResidue
CCYS38
CSER40
CHIS62
CASP153
CTRP295
CZN502
CNAD503
CMPD505

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD C 505
ChainResidue
CMET47
CTYR54
CILE271
CACY504

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 501
ChainResidue
DCYS92
DCYS95
DCYS98
DCYS106

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 502
ChainResidue
DCYS38
DHIS62
DASP153
DNAD503
DACY504

site_idBC9
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAD D 503
ChainResidue
APHE281
DHIS39
DSER40
DASP153
DTHR157
DGLY179
DVAL180
DGLY181
DGLY182
DLEU183
DASP203
DLEU204
DARG208
DSER223
DPHE246
DVAL247
DTHR252
DVAL269
DGLY270
DILE271
DPRO293
DTYR294
DTRP295
DLEU332
DARG340
DHOH354
DHOH361
DHOH384
DHOH386
DHOH416
DHOH418
DHOH421
DHOH429
DHOH439
DHOH453
DZN502
DACY504

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY D 504
ChainResidue
DCYS38
DSER40
DHIS62
DASP153
DTRP295
DZN502
DNAD503
DMPD505

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD D 505
ChainResidue
DPHE43
DTYR54
DILE271
DHOH459
DACY504

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGTvaelGegV
ChainResidueDetails
AGLY61-VAL75

227344

PDB entries from 2024-11-13

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