1XG4

Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant from Escherichia coli in complex with the inhibitor isocitrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
A	0046421	molecular_function	methylisocitrate lyase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
B	0046421	molecular_function	methylisocitrate lyase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
C	0046421	molecular_function	methylisocitrate lyase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0016829	molecular_function	lyase activity
D	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
D	0046421	molecular_function	methylisocitrate lyase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1101

Chain	Residue
A	ASP85
A	ICT1105
A	HOH1360
A	HOH1361
A	HOH1362

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1201

Chain	Residue
B	HOH1467
B	ASP85
B	ICT1205
B	HOH1465
B	HOH1466

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1401

Chain	Residue
D	ASP85
D	ICT1405
D	HOH1633
D	HOH1634
D	HOH1635

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ICT A 1105

Chain	Residue
A	SER45
A	GLY46
A	GLY47
A	ASP85
A	SER123
A	GLY124
A	HIS125
A	ARG158
A	GLU188
A	ASN210
A	THR212
A	PRO236
A	ARG241
A	MG1101
A	HOH1360
B	ARG270

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT B 1205

Chain	Residue
A	ARG270
B	SER45
B	GLY46
B	GLY47
B	ASP85
B	SER123
B	GLY124
B	HIS125
B	ARG158
B	GLU188
B	ASN210
B	THR212
B	PRO236
B	ARG241
B	MG1201
B	HOH1230
B	HOH1465

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT D 1405

Chain	Residue
C	ARG270
D	SER45
D	GLY46
D	GLY47
D	ASP85
D	SER123
D	GLY124
D	HIS125
D	ARG158
D	GLU188
D	ASN210
D	THR212
D	PRO236
D	ARG241
D	MG1401
D	HOH1436
D	HOH1633

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01939","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15723538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01939","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12706720","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15723538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 182

Chain	Residue	Details
A	TYR43	proton acceptor, proton donor
A	ASN210	electrostatic stabiliser, hydrogen bond donor
A	ASP58	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP85	metal ligand
A	ASP87	metal ligand
A	HIS113	proton acceptor, proton donor, proton relay
A	GLU115	proton acceptor, proton donor, proton relay
A	SER123	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG158	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
A	GLU188	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	10
Details	M-CSA 182

Chain	Residue	Details
B	TYR43	proton acceptor, proton donor
B	ASN210	electrostatic stabiliser, hydrogen bond donor
B	ASP58	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP85	metal ligand
B	ASP87	metal ligand
B	HIS113	proton acceptor, proton donor, proton relay
B	GLU115	proton acceptor, proton donor, proton relay
B	SER123	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG158	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
B	GLU188	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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site_id	MCSA3
Number of Residues	10
Details	M-CSA 182

Chain	Residue	Details
C	TYR43	proton acceptor, proton donor
C	ASN210	electrostatic stabiliser, hydrogen bond donor
C	ASP58	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP85	metal ligand
C	ASP87	metal ligand
C	HIS113	proton acceptor, proton donor, proton relay
C	GLU115	proton acceptor, proton donor, proton relay
C	SER123	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG158	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
C	GLU188	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

---

site_id	MCSA4
Number of Residues	10
Details	M-CSA 182

Chain	Residue	Details
D	TYR43	proton acceptor, proton donor
D	ASN210	electrostatic stabiliser, hydrogen bond donor
D	ASP58	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP85	metal ligand
D	ASP87	metal ligand
D	HIS113	proton acceptor, proton donor, proton relay
D	GLU115	proton acceptor, proton donor, proton relay
D	SER123	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG158	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
D	GLU188	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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