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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SMZ

Crystal structure of SLA Reductase YihU from E. Coli in complex with NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0009407biological_processtoxin catabolic process
A0016054biological_processorganic acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0047577molecular_function4-hydroxybutyrate dehydrogenase activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0051289biological_processprotein homotetramerization
A0061596molecular_function3-sulfolactaldehyde reductase activity
A0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
A1902777biological_process6-sulfoquinovose(1-) catabolic process
B0009407biological_processtoxin catabolic process
B0016054biological_processorganic acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0047577molecular_function4-hydroxybutyrate dehydrogenase activity
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0051289biological_processprotein homotetramerization
B0061596molecular_function3-sulfolactaldehyde reductase activity
B0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
B1902777biological_process6-sulfoquinovose(1-) catabolic process
C0009407biological_processtoxin catabolic process
C0016054biological_processorganic acid catabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0047577molecular_function4-hydroxybutyrate dehydrogenase activity
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0051289biological_processprotein homotetramerization
C0061596molecular_function3-sulfolactaldehyde reductase activity
C0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
C1902777biological_process6-sulfoquinovose(1-) catabolic process
D0009407biological_processtoxin catabolic process
D0016054biological_processorganic acid catabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0047577molecular_function4-hydroxybutyrate dehydrogenase activity
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0051289biological_processprotein homotetramerization
D0061596molecular_function3-sulfolactaldehyde reductase activity
D0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
D1902777biological_process6-sulfoquinovose(1-) catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY10
AVAL74
ASER95
ATHR96
AVAL121
AARG123
AHOH509
AHOH510
AHOH526
AHOH534
AHOH562
AGLN11
AHOH563
BHOH511
BHOH514
BHOH568
BHOH585
AMET12
AGLY13
APHE30
AASP31
AVAL32
AMET64
ALEU65
site_idAC2
Number of Residues25
Detailsbinding site for residue NAD C 401
ChainResidue
CGLY10
CGLN11
CMET12
CGLY13
CPHE30
CASP31
CVAL32
CMET64
CLEU65
CVAL74
CSER95
CTHR96
CVAL121
CARG123
CHOH511
CHOH518
CHOH524
CHOH525
CHOH537
CHOH538
CHOH552
CHOH597
DHOH523
DHOH530
DHOH612
site_idAC3
Number of Residues20
Detailsbinding site for residue NAD B 401
ChainResidue
AHOH608
BGLY10
BGLN11
BMET12
BASP31
BVAL32
BMET64
BLEU65
BVAL74
BSER95
BTHR96
BVAL121
BARG123
BHOH503
BHOH512
BHOH534
BHOH536
BHOH539
BHOH556
BHOH580
site_idAC4
Number of Residues18
Detailsbinding site for residue NAD D 401
ChainResidue
DGLY10
DGLN11
DMET12
DPHE30
DASP31
DVAL32
DMET64
DLEU65
DVAL74
DTHR96
DVAL121
DARG123
DLYS171
DHOH505
DHOH508
DHOH509
DHOH546
DHOH557
Functional Information from PROSITE/UniProt
site_idPS00895
Number of Residues14
Details3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGqMGspMAsN
ChainResidueDetails
APHE6-ASN19
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01913","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2020","firstPage":"2826","lastPage":"2836","volume":"10","journal":"ACS Catal.","title":"Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase.","authors":["Sharma M.","Abayakoon P.","Lingford J.P.","Epa R.","John A.","Jin Y.","Goddard-Borger E.D.","Davies G.J.","Williams S.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.9b04427"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01913","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2020","firstPage":"2826","lastPage":"2836","volume":"10","journal":"ACS Catal.","title":"Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase.","authors":["Sharma M.","Abayakoon P.","Lingford J.P.","Epa R.","John A.","Jin Y.","Goddard-Borger E.D.","Davies G.J.","Williams S.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.9b04427"}]}},{"source":"PDB","id":"6SMY","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6SMZ","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01913","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2020","firstPage":"2826","lastPage":"2836","volume":"10","journal":"ACS Catal.","title":"Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase.","authors":["Sharma M.","Abayakoon P.","Lingford J.P.","Epa R.","John A.","Jin Y.","Goddard-Borger E.D.","Davies G.J.","Williams S.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.9b04427"}]}},{"source":"PDB","id":"6SMY","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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