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6UHX

Crystal structure of YIR035C short chain dehydrogenases/reductase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008150biological_processbiological_process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
A0102306molecular_functionbenzil reductase [(S)-benzoin-forming] activity
B0005737cellular_componentcytoplasm
B0008150biological_processbiological_process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B0102306molecular_functionbenzil reductase [(S)-benzoin-forming] activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAP A 301
ChainResidue
AGLY9
AASN85
AALA86
AGLY87
AILE109
ASER136
ASER137
ATYR150
ALYS154
APRO178
AGLY179
ASER11
AVAL181
ATHR183
AMET185
AGLN186
AARG12
AILE14
AARG36
ASER37
AGLY57
AASP58
AILE59

site_idAC2
Number of Residues26
Detailsbinding site for residue NAP B 301
ChainResidue
BGLY9
BSER11
BARG12
BGLY13
BILE14
BALA35
BARG36
BSER37
BASP58
BILE59
BASN85
BALA86
BGLY87
BVAL135
BSER136
BSER137
BTYR150
BLYS154
BPRO178
BGLY179
BVAL181
BTHR183
BASP184
BMET185
BGLN186
BHOH421

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SdacnmyfssWgaYGSSKAALnHFAmTLA
ChainResidueDetails
ASER137-ALA165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O93868
ChainResidueDetails
ASER136
BSER136

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:O93868
ChainResidueDetails
ALYS154
BLYS154

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4
ChainResidueDetails
AVAL7
ATHR183
BVAL7
BTHR183

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O93868
ChainResidueDetails
AASN85
ATYR150
ALYS154
AVAL181
BASN85
BTYR150
BLYS154
BVAL181

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PDB entries from 2024-11-06

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