Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YVE

ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIUM AND INHIBITOR IPOHA (N-HYDROXY-N-ISOPROPYLOXAMATE)

Functional Information from GO Data

Chain	GOid	namespace	contents
I	0004455	molecular_function	ketol-acid reductoisomerase activity
I	0009082	biological_process	branched-chain amino acid biosynthetic process
I	0016491	molecular_function	oxidoreductase activity
J	0004455	molecular_function	ketol-acid reductoisomerase activity
J	0009082	biological_process	branched-chain amino acid biosynthetic process
J	0016491	molecular_function	oxidoreductase activity
K	0004455	molecular_function	ketol-acid reductoisomerase activity
K	0009082	biological_process	branched-chain amino acid biosynthetic process
K	0016491	molecular_function	oxidoreductase activity
L	0004455	molecular_function	ketol-acid reductoisomerase activity
L	0009082	biological_process	branched-chain amino acid biosynthetic process
L	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG I 601

Chain	Residue
I	ASP315
I	GLU319
I	HIO603
I	HOH899
I	HOH900

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG I 602

Chain	Residue
I	HOH897
I	ASP315
I	HIO603
I	HOH895
I	HOH896

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL I 604

Chain	Residue
I	GLN142
I	ARG259

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG J 601

Chain	Residue
J	ASP315
J	GLU319
J	HIO603
J	HOH930
L	HOH796

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG J 602

Chain	Residue
J	ASP315
J	HIO603
J	HOH926
J	HOH927
J	HOH928

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL J 604

Chain	Residue
J	ARG259
J	HOH607

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG K 601

Chain	Residue
K	HIS226
K	ASP315
K	NDP600
K	HIO603
K	HOH715
K	HOH716

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG K 602

Chain	Residue
K	ASP315
K	HIO603
K	HOH717
K	HOH718
K	HOH719

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL K 604

Chain	Residue
K	ARG259

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG L 601

Chain	Residue
L	ASP315
L	GLU319
L	HIO603
L	HOH817
L	HOH818

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG L 602

Chain	Residue
L	ASP315
L	HIO603
L	HOH813
L	HOH814
L	HOH815

site_id	BC3
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NDP I 600

Chain	Residue
I	GLY132
I	TRP133
I	GLY134
I	SER135
I	GLN136
I	ARG162
I	SER165
I	SER167
I	MET186
I	LEU199
I	ILE200
I	SER201
I	ASP202
I	ALA204
I	GLN205
I	SER225
I	HIS226
I	PRO251
I	GLY253
I	MET254
I	GLY255
I	CYS517
I	SER518
I	THR519
I	ARG589
I	HIO603
I	HOH759
I	HOH762
I	HOH763
I	HOH772
I	HOH899
I	HOH901
I	HOH916
I	HOH921
I	HOH940

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HIO I 603

Chain	Residue
I	MET254
I	ASP315
I	GLU319
I	GLU496
I	LEU501
I	CYS517
I	SER518
I	ALA521
I	NDP600
I	MG601
I	MG602
I	HOH896
I	HOH897
I	HOH899
I	HOH900

site_id	BC5
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NDP K 600

Chain	Residue
K	SER135
K	GLN136
K	ARG162
K	SER165
K	SER167
K	LEU199
K	ILE200
K	SER201
K	ASP202
K	ALA204
K	GLN205
K	SER225
K	HIS226
K	PRO251
K	MET254
K	GLY255
K	CYS517
K	SER518
K	THR519
K	ARG589
K	MG601
K	HIO603
K	HOH642
K	HOH701
K	HOH704
K	HOH709
K	HOH714
K	HOH902
K	HOH905
K	HOH906
K	HOH907
K	GLY132
K	TRP133
K	GLY134

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HIO J 603

Chain	Residue
J	MET254
J	ASP315
J	GLU319
J	GLU496
J	LEU501
J	CYS517
J	SER518
J	ALA521
J	MG601
J	MG602
J	HOH927
J	HOH928
L	NDP600
L	HOH796

site_id	BC7
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NDP K 605

Chain	Residue
K	HOH621
K	HOH775
K	HOH983
K	HOH984
K	HOH985
K	HOH986
K	HOH987
L	GLY132
L	TRP133
L	GLY134
L	SER135
L	GLN136
L	ARG162
L	SER165
L	SER167
L	LEU199
L	ILE200
L	SER201
L	ASP202
L	ALA204
L	GLN205
L	SER225
L	HIS226
L	PRO251
L	GLY253
L	MET254
L	GLY255
L	CYS517
L	SER518
L	THR519
L	ARG589
L	HIO603
L	HOH658
L	HOH817
L	HOH984

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HIO K 603

Chain	Residue
K	MET254
K	ASP315
K	GLU319
K	GLU496
K	LEU501
K	CYS517
K	SER518
K	ALA521
K	NDP600
K	MG601
K	MG602
K	HOH715
K	HOH717
K	HOH719

site_id	BC9
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NDP L 600

Chain	Residue
J	TRP133
J	GLY134
J	SER135
J	GLN136
J	ARG162
J	SER165
J	SER167
J	LEU199
J	ILE200
J	SER201
J	ASP202
J	ALA204
J	GLN205
J	SER225
J	HIS226
J	PRO251
J	MET254
J	GLY255
J	CYS517
J	SER518
J	THR519
J	ARG589
J	HIO603
J	HOH614
J	HOH977
L	HOH629
L	HOH630
L	HOH631
L	HOH796
L	HOH797
L	HOH798
L	HOH799
L	HOH800
L	HOH801

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HIO L 603

Chain	Residue
K	NDP605
L	GLY253
L	MET254
L	ASP315
L	GLU319
L	GLU496
L	LEU501
L	CYS517
L	SER518
L	ALA521
L	MG601
L	MG602
L	HOH814
L	HOH815
L	HOH817
L	HOH818

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
I	HIS226
J	HIS226
K	HIS226
L	HIS226

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:10739911, ECO:0000269\|PubMed:9218783

Chain	Residue	Details
I	GLY129
L	GLY129
L	ARG162
L	SER201
I	ARG162
I	SER201
J	GLY129
J	ARG162
J	SER201
K	GLY129
K	ARG162
K	SER201

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01198

Chain	Residue	Details
I	ASP315
J	SER518
K	ASP315
K	GLU319
K	GLU492
K	GLU496
K	SER518
L	ASP315
L	GLU319
L	GLU492
L	GLU496
I	GLU319
L	SER518
I	GLU492
I	GLU496
I	SER518
J	ASP315
J	GLU319
J	GLU492
J	GLU496

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 890

Chain	Residue	Details
I	LYS252	proton acceptor, proton donor
I	ASP315	metal ligand
I	GLU319	metal ligand

site_id	MCSA2
Number of Residues	3
Details	M-CSA 890

Chain	Residue	Details
J	LYS252	proton acceptor, proton donor
J	ASP315	metal ligand
J	GLU319	metal ligand

site_id	MCSA3
Number of Residues	3
Details	M-CSA 890

Chain	Residue	Details
K	LYS252	proton acceptor, proton donor
K	ASP315	metal ligand
K	GLU319	metal ligand

site_id	MCSA4
Number of Residues	3
Details	M-CSA 890

Chain	Residue	Details
L	LYS252	proton acceptor, proton donor
L	ASP315	metal ligand
L	GLU319	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)