1SR9

Crystal Structure of LeuA 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	0003852	molecular_function	2-isopropylmalate synthase activity
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0008270	molecular_function	zinc ion binding
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030145	molecular_function	manganese ion binding
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding
A	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003852	molecular_function	2-isopropylmalate synthase activity
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0008270	molecular_function	zinc ion binding
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030145	molecular_function	manganese ion binding
B	0030955	molecular_function	potassium ion binding
B	0046872	molecular_function	metal ion binding
B	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 703

Chain	Residue
B	ASP81
B	HIS285
B	HIS287
B	KIV702
B	HOH1257

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 704

Chain	Residue
A	HOH1108
A	ASP81
A	HIS285
A	HIS287
A	KIV701

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 705

Chain	Residue
A	GLY533
A	PRO534
A	LEU535
B	ILE627

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE KIV A 701

Chain	Residue
A	ARG80
A	ASP81
A	HIS167
A	SER216
A	GLU218
A	PRO252
A	THR254
A	HIS285
A	HIS287
A	ZN704
A	HOH1019

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE KIV B 702

Chain	Residue
B	ARG80
B	ASP81
B	GLU218
B	PRO252
B	THR254
B	HIS285
B	HIS287
B	ZN703
B	HOH1029
B	HOH1257

---

Functional Information from PROSITE/UniProt

site_id	PS00815
Number of Residues	17
Details	AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGnQalidPmsparK

Chain	Residue	Details
A	LEU79-LYS95

---

site_id	PS00816
Number of Residues	14
Details	AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. LslHpHNDrGtAvA

Chain	Residue	Details
A	LEU282-ALA295

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Repeat: {"description":"VNTR1","evidences":[{"source":"PubMed","id":"11914056","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00572","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HQ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3U6W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00572","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3HPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HQ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SR9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3U6W","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FIG","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---