Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YRL

Escherichia coli ketol-acid reductoisomerase

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	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0008677	molecular_function	2-dehydropantoate 2-reductase activity
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	0015940	biological_process	pantothenate biosynthetic 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	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	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0008677	molecular_function	2-dehydropantoate 2-reductase activity
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	0015940	biological_process	pantothenate biosynthetic 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	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	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0008677	molecular_function	2-dehydropantoate 2-reductase activity
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	0015940	biological_process	pantothenate biosynthetic 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	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	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008652	biological_process	amino acid biosynthetic process
D	0008677	molecular_function	2-dehydropantoate 2-reductase activity
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	0015940	biological_process	pantothenate biosynthetic 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	0046872	molecular_function	metal ion binding
D	0050661	molecular_function	NADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 4121

Chain	Residue
A	ASN3
A	ASN6
A	HOH4183
A	HOH4282

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 4122

Chain	Residue
A	ARG11
A	GLN12

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 4123

Chain	Residue
D	ASN3
D	ASN6

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 4124

Chain	Residue
D	ARG11
D	GLN12
A	GLN301

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 4125

Chain	Residue
C	ARG11
C	GLN12

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 4126

Chain	Residue
B	ARG11
B	GLN12

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 4127

Chain	Residue
A	ALA71
A	ARG76
A	SER78
A	HOH4156
A	HOH4163

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 4128

Chain	Residue
A	HIS201
A	ARG202

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 4129

Chain	Residue
D	HIS201
D	ARG202

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00435

Chain	Residue	Details
A	GLY133
B	GLY133
C	GLY133
D	GLY133

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00435, ECO:0000269\|PubMed:23036858

Chain	Residue	Details
A	GLY46
B	LEU218
B	SER390
B	LEU394
C	GLY46
C	TRP79
C	LYS109
C	LEU218
C	SER390
C	LEU394
D	GLY46
A	TRP79
D	TRP79
D	LYS109
D	LEU218
D	SER390
D	LEU394
A	LYS109
A	LEU218
A	SER390
A	LEU394
B	GLY46
B	TRP79
B	LYS109

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00435, ECO:0000305\|PubMed:9015391

Chain	Residue	Details
A	LYS69
B	LYS69
C	LYS69
D	LYS69

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00435, ECO:0000269\|PubMed:23036858, ECO:0000305\|PubMed:9015391

Chain	Residue	Details
A	ALA77
B	ALA77
C	ALA77
D	ALA77

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00435

Chain	Residue	Details
A	THR159
D	THR159
D	GLN222
D	ASP415
A	GLN222
A	ASP415
B	THR159
B	GLN222
B	ASP415
C	THR159
C	GLN222
C	ASP415

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
A	GLU393

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
B	GLU393

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
C	GLU393

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
D	GLU393

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
A	GLU383

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
B	GLU383

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
C	GLU383

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1yve

Chain	Residue	Details
D	GLU383

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)