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5OD3

Crystal structure of R. ruber ADH-A, mutant Y54G, L119Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
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
ASER40
AHIS62
AASP153
ANAD503

site_idAC3
Number of Residues35
Detailsbinding site for residue NAD A 503
ChainResidue
ACYS38
AHIS39
ASER40
AASP153
ATHR157
AVAL180
AGLY181
AGLY182
ALEU183
AASP203
ALEU204
AARG208
ASER223
APHE246
AVAL247
ATHR252
AVAL269
AGLY270
AILE271
APRO293
ATYR294
ATRP295
ALEU332
AARG340
AZN502
AHOH656
AHOH658
AHOH693
AHOH706
AHOH718
AHOH727
AHOH739
AHOH793
AHOH809
DPHE281

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS92
BCYS95
BCYS98
BCYS106

site_idAC5
Number of Residues6
Detailsbinding site for residue ZN B 502
ChainResidue
BCYS38
BSER40
BHIS62
BASP153
BNAD503
BHOH791

site_idAC6
Number of Residues34
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
BZN502
BHOH618
BHOH632
BHOH633
BHOH692
BHOH721
BHOH722
BHOH726
BHOH750
BHOH791
BHOH800
CPHE281

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN C 501
ChainResidue
CCYS92
CCYS95
CCYS98
CCYS106

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN C 502
ChainResidue
CCYS38
CHIS62
CASP153
CNAD503

site_idAC9
Number of Residues37
Detailsbinding site for residue NAD C 503
ChainResidue
CASP153
CTHR157
CVAL180
CGLY181
CGLY182
CLEU183
CASP203
CLEU204
CARG208
CSER223
CPHE246
CVAL247
CTHR252
CVAL269
CGLY270
CILE271
CPRO293
CTYR294
CTRP295
CLEU332
CARG340
CZN502
CHOH608
CHOH622
CHOH649
CHOH652
CHOH667
CHOH675
CHOH679
CHOH722
CHOH739
CHOH741
CHOH768
CHOH782
CCYS38
CHIS39
CSER40

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN D 501
ChainResidue
DCYS92
DCYS95
DCYS98
DCYS106

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN D 502
ChainResidue
DCYS38
DHIS62
DASP153
DNAD503
DHOH744

site_idAD3
Number of Residues34
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
DZN502
DHOH629
DHOH631
DHOH648
DHOH684
DHOH712
DHOH727
DHOH743
DHOH761

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

219869

PDB entries from 2024-05-15

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