6T4V

Crystal structure of 2-methylisocitrate lyase (PrpB) from Pseudomonas aeruginosa in apo form.

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	0016833	molecular_function	oxo-acid-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	0016833	molecular_function	oxo-acid-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	0016833	molecular_function	oxo-acid-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	0016833	molecular_function	oxo-acid-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	6
Details	binding site for residue PYR C 301

Chain	Residue
C	LEU66
C	PHE92
C	ASN98
C	ARG101
C	THR102
D	ILE63

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site_id	AC2
Number of Residues	6
Details	binding site for residue PYR A 301

Chain	Residue
A	ARG101
A	THR102
B	ILE63
A	LEU66
A	PHE92
A	ASN98

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site_id	AC3
Number of Residues	6
Details	binding site for residue PYR B 301

Chain	Residue
A	ILE63
B	PHE92
B	ASN98
B	ARG101
B	THR102
B	HOH486

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site_id	AC4
Number of Residues	6
Details	binding site for residue PYR D 301

Chain	Residue
C	ILE63
D	PHE92
D	ASN98
D	ARG101
D	THR102
D	HOH455

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Functional Information from PROSITE/UniProt

site_id	PS00161
Number of Residues	6
Details	ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR

Chain	Residue	Details
C	LYS123-ARG128

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