4XIY

Crystal structure of ketol-acid reductoisomerase from Azotobacter

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004455	molecular_function	ketol-acid reductoisomerase activity
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0050661	molecular_function	NADP binding
B	0000287	molecular_function	magnesium ion binding
B	0004455	molecular_function	ketol-acid reductoisomerase activity
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0050661	molecular_function	NADP binding
C	0000287	molecular_function	magnesium ion binding
C	0004455	molecular_function	ketol-acid reductoisomerase activity
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009097	biological_process	isoleucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0050661	molecular_function	NADP binding
D	0000287	molecular_function	magnesium ion binding
D	0004455	molecular_function	ketol-acid reductoisomerase activity
D	0005829	cellular_component	cytosol
D	0008652	biological_process	amino acid biosynthetic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009097	biological_process	isoleucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0050661	molecular_function	NADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 401

Chain	Residue
A	GLU226
A	GLU230
B	ASP190
B	HOH506
B	HOH507

---

site_id	AC2
Number of Residues	2
Details	binding site for residue FE A 402

Chain	Residue
A	ASP190
A	GLU194

---

site_id	AC3
Number of Residues	3
Details	binding site for residue PGE A 403

Chain	Residue
A	ARG305
A	TYR298
A	THR302

---

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 401

Chain	Residue
A	ASP190
B	GLU226
B	GLU230

---

site_id	AC5
Number of Residues	5
Details	binding site for residue FE B 402

Chain	Residue
B	ASP190
B	GLU194
B	HOH501
B	HOH503
B	HOH504

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PGE B 403

Chain	Residue
A	ASN252
B	TYR298
B	THR302
B	ARG305

---

site_id	AC7
Number of Residues	3
Details	binding site for residue FE C 401

Chain	Residue
C	ASP190
C	GLU194
C	HOH501

---

site_id	AC8
Number of Residues	5
Details	binding site for residue MG C 402

Chain	Residue
C	GLU226
C	GLU230
C	HOH506
D	ASP190
D	HOH509

---

site_id	AC9
Number of Residues	3
Details	binding site for residue PEG C 403

Chain	Residue
C	TYR298
C	THR302
C	ARG305

---

site_id	AD1
Number of Residues	3
Details	binding site for residue MG D 401

Chain	Residue
C	ASP190
D	GLU226
D	GLU230

---

site_id	AD2
Number of Residues	6
Details	binding site for residue FE D 402

Chain	Residue
C	HOH505
D	ASP190
D	GLU194
D	HOH502
D	HOH503
D	HOH508

---

site_id	AD3
Number of Residues	4
Details	binding site for residue PG4 D 403

Chain	Residue
C	TYR248
D	TYR298
D	THR302
D	ARG305

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	720
Details	Domain: {"description":"KARI N-terminal Rossmann","evidences":[{"source":"PROSITE-ProRule","id":"PRU01197","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	580
Details	Domain: {"description":"KARI C-terminal knotted","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25849365","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25849365","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---