6SM7

Crystal structure of SLA Reductase YihU from E. Coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009407	biological_process	toxin catabolic process
A	0016054	biological_process	organic acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0047577	molecular_function	4-hydroxybutyrate dehydrogenase activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0051289	biological_process	protein homotetramerization
A	0061596	molecular_function	3-sulfolactaldehyde reductase activity
A	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
A	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
B	0009407	biological_process	toxin catabolic process
B	0016054	biological_process	organic acid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0047577	molecular_function	4-hydroxybutyrate dehydrogenase activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
B	0051289	biological_process	protein homotetramerization
B	0061596	molecular_function	3-sulfolactaldehyde reductase activity
B	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
B	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
C	0009407	biological_process	toxin catabolic process
C	0016054	biological_process	organic acid catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0047577	molecular_function	4-hydroxybutyrate dehydrogenase activity
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
C	0051289	biological_process	protein homotetramerization
C	0061596	molecular_function	3-sulfolactaldehyde reductase activity
C	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
C	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
D	0009407	biological_process	toxin catabolic process
D	0016054	biological_process	organic acid catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0047577	molecular_function	4-hydroxybutyrate dehydrogenase activity
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding
D	0051289	biological_process	protein homotetramerization
D	0061596	molecular_function	3-sulfolactaldehyde reductase activity
D	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
D	1902777	biological_process	6-sulfoquinovose(1-) catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue BO3 A 401

Chain	Residue
A	PHE233
A	LYS240
A	ASP241
A	HOH514
A	HOH578
A	HOH614

---

site_id	AC2
Number of Residues	6
Details	binding site for residue BO3 B 401

Chain	Residue
B	HOH524
B	HOH529
B	HOH532
B	PHE233
B	LYS240
B	ASP241

---

site_id	AC3
Number of Residues	6
Details	binding site for residue BO3 D 401

Chain	Residue
D	PHE233
D	LYS240
D	ASP241
D	HOH536
D	HOH541
D	HOH570

---

site_id	AC4
Number of Residues	7
Details	binding site for residue BO3 C 401

Chain	Residue
C	PHE233
C	LYS240
C	ASP241
C	HOH533
C	HOH536
C	HOH548
D	ASN175

---

Functional Information from PROSITE/UniProt

site_id	PS00895
Number of Residues	14
Details	3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGqMGspMAsN

Chain	Residue	Details
A	PHE6-ASN19

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active 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"}]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding 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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding 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"}]}

Chain

Residue

Details

---