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1ZK3

Triclinic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0016491molecular_functionoxidoreductase activity
G0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0016491molecular_functionoxidoreductase activity
H0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 3252
ChainResidue
AGLN251
AHOH329
AHOH656
CGLN251
CHOH256
CHOH683

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 3253
ChainResidue
DGLN251
DHOH456
DHOH529
BGLN251
BHOH483
BHOH856

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG G 3254
ChainResidue
EGLN251
EHOH1056
EHOH1083
GGLN251
GHOH1129
GHOH1456
GHOH1483

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG H 3255
ChainResidue
FGLN251
FHOH1256
FHOH1283
HGLN251
HHOH1329
HHOH1656
HHOH1683

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SiegfvgdpsLgaYNASKGAVrIMSkSAA
ChainResidueDetails
ASER142-ALA170

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR155
ASER142
AGLU144
ALYS159

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BSER142
BTYR155
BLYS159

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
CSER142
CTYR155
CLYS159

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
DSER142
DTYR155
DLYS159

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ESER142
ETYR155
ELYS159

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
FSER142
FTYR155
FLYS159

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
GSER142
GTYR155
GLYS159

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
HSER142
HTYR155
HLYS159

site_idCSA17
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR155
ASER142
AASN113
ALYS159

site_idCSA18
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR155
BSER142
BASN113
BLYS159

site_idCSA19
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
CTYR155
CSER142
CASN113
CLYS159

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR155
BSER142
BGLU144
BLYS159

site_idCSA20
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
DTYR155
DSER142
DASN113
DLYS159

site_idCSA21
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ETYR155
ESER142
EASN113
ELYS159

site_idCSA22
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
FTYR155
FSER142
FASN113
FLYS159

site_idCSA23
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
GTYR155
GSER142
GASN113
GLYS159

site_idCSA24
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
HTYR155
HSER142
HASN113
HLYS159

site_idCSA25
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ALEU152
ALYS159

site_idCSA26
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BLEU152
BLYS159

site_idCSA27
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
CLEU152
CLYS159

site_idCSA28
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
DLEU152
DLYS159

site_idCSA29
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ELEU152
ELYS159

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
CTYR155
CSER142
CGLU144
CLYS159

site_idCSA30
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
FLEU152
FLYS159

site_idCSA31
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
GLEU152
GLYS159

site_idCSA32
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
HLEU152
HLYS159

site_idCSA33
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR155
ALYS159

site_idCSA34
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR155
BLYS159

site_idCSA35
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
CTYR155
CLYS159

site_idCSA36
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
DTYR155
DLYS159

site_idCSA37
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ETYR155
ELYS159

site_idCSA38
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
FTYR155
FLYS159

site_idCSA39
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
GTYR155
GLYS159

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
DTYR155
DSER142
DGLU144
DLYS159

site_idCSA40
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
HTYR155
HLYS159

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ETYR155
ESER142
EGLU144
ELYS159

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
FTYR155
FSER142
FGLU144
FLYS159

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
GTYR155
GSER142
GGLU144
GLYS159

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
HTYR155
HSER142
HGLU144
HLYS159

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ASER142
ATYR155
ALYS159

223166

PDB entries from 2024-07-31

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