Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OVT

Crystal Structure of IlvD from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004160	molecular_function	dihydroxy-acid dehydratase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
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	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004160	molecular_function	dihydroxy-acid dehydratase activity
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
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	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004160	molecular_function	dihydroxy-acid dehydratase activity
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
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	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004160	molecular_function	dihydroxy-acid dehydratase activity
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
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	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 601

Chain	Residue
A	ASP96
A	ASP138
A	KCX139
A	GLU465
A	HOH707
A	HOH737

site_id	AC2
Number of Residues	9
Details	binding site for residue FES A 602

Chain	Residue
A	GLY97
A	CYS137
A	ASP138
A	CYS214
A	HOH861
C	MET36
A	CYS64
A	SER95
A	ASP96

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 603

Chain	Residue
A	ASP69
A	HOH775
A	HOH932
A	HOH936
A	HOH965
A	HOH1014

site_id	AC4
Number of Residues	6
Details	binding site for residue MG A 604

Chain	Residue
A	HOH713
A	HOH824
A	HOH841
A	HOH1058
A	HOH1072
A	HOH1082

site_id	AC5
Number of Residues	5
Details	binding site for residue PEG A 605

Chain	Residue
A	GLY354
A	LEU355
A	LEU356
A	HIS357
A	HOH945

site_id	AC6
Number of Residues	6
Details	binding site for residue MG B 601

Chain	Residue
B	ASP96
B	ASP138
B	KCX139
B	GLU465
B	HOH810
B	HOH905

site_id	AC7
Number of Residues	8
Details	binding site for residue FES B 602

Chain	Residue
B	CYS64
B	GLY97
B	CYS137
B	ASP138
B	ALA213
B	CYS214
B	HOH859
D	MET36

site_id	AC8
Number of Residues	5
Details	binding site for residue PEG B 603

Chain	Residue
B	ILE316
B	GLY354
B	LEU355
B	LEU356
B	HIS357

site_id	AC9
Number of Residues	6
Details	binding site for residue MG B 604

Chain	Residue
B	ASP69
B	HOH755
B	HOH759
B	HOH819
B	HOH898
B	HOH921

site_id	AD1
Number of Residues	6
Details	binding site for residue MG B 605

Chain	Residue
B	HOH715
B	HOH842
B	HOH846
B	HOH945
B	HOH947
B	HOH956

site_id	AD2
Number of Residues	7
Details	binding site for residue FES C 601

Chain	Residue
C	CYS64
C	GLY97
C	CYS137
C	ASP138
C	ALA213
C	CYS214
C	HOH840

site_id	AD3
Number of Residues	4
Details	binding site for residue PEG C 602

Chain	Residue
C	ILE316
C	LEU355
C	LEU356
C	HIS357

site_id	AD4
Number of Residues	6
Details	binding site for residue MG C 603

Chain	Residue
C	ASP96
C	ASP138
C	KCX139
C	GLU465
C	HOH829
C	HOH926

site_id	AD5
Number of Residues	6
Details	binding site for residue MG C 604

Chain	Residue
C	ASP69
C	HOH847
C	HOH851
C	HOH869
C	HOH874
C	HOH961

site_id	AD6
Number of Residues	6
Details	binding site for residue MG C 605

Chain	Residue
C	HOH723
C	HOH802
C	HOH886
C	HOH986
C	HOH993
C	HOH1005

site_id	AD7
Number of Residues	6
Details	binding site for residue MG D 601

Chain	Residue
D	ASP96
D	ASP138
D	KCX139
D	GLU465
D	HOH905
D	HOH906

site_id	AD8
Number of Residues	6
Details	binding site for residue MG D 602

Chain	Residue
D	HOH770
D	HOH868
D	HOH899
D	HOH926
D	HOH964
D	ASP69

site_id	AD9
Number of Residues	8
Details	binding site for residue FES D 603

Chain	Residue
B	MET36
D	CYS64
D	GLY97
D	CYS137
D	ASP138
D	ALA213
D	CYS214
D	HOH922

site_id	AE1
Number of Residues	6
Details	binding site for residue MG D 604

Chain	Residue
A	HOH743
A	HOH1080
D	HOH727
D	HOH733
D	HOH918
D	HOH1002

site_id	AE2
Number of Residues	4
Details	binding site for residue NA D 605

Chain	Residue
D	ASP430
D	GLY431
D	ARG433
D	ALA434

Functional Information from PROSITE/UniProt

site_id	PS00626
Number of Residues	11
Details	RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IGSGvPHLADV

Chain	Residue	Details
A	ILE316-VAL326

site_id	PS00886
Number of Residues	11
Details	ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKslPGmlmA

Chain	Residue	Details
A	CYS137-ALA147

site_id	PS00887
Number of Residues	12
Details	ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. LLLTDGRFSGGT

Chain	Residue	Details
A	LEU483-THR494

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"31315931","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"31315931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OVT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"31315931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OVT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"31315931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OVT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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