4IF2

Structure of the phosphotriesterase from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0009056	biological_process	catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HIS22
A	HIS24
A	KCX145
A	ASP264
A	ZN402

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	ZN401
A	HOH508
A	KCX145
A	HIS178
A	HIS207
A	ARG231

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Functional Information from PROSITE/UniProt

site_id	PS00962
Number of Residues	12
Details	RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. LeELIAAGSYLG

Chain	Residue	Details
A	LEU217-GLY228

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site_id	PS01322
Number of Residues	9
Details	PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GvTLmHEHV

Chain	Residue	Details
A	GLY17-VAL25

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2

Chain	Residue	Details
A	HIS22
A	HIS24
A	HIS178
A	HIS207
A	ASP264

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: via carbamate group => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2

Chain	Residue	Details
A	KCX145

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2

Chain	Residue	Details
A	KCX145

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