3A8H

Crystal structure of Nitrile Hydratase mutant S113A complexed with Trimethylacetamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0018822	molecular_function	nitrile hydratase activity
A	0046872	molecular_function	metal ion binding
A	0046914	molecular_function	transition metal ion binding
B	0016829	molecular_function	lyase activity
B	0018822	molecular_function	nitrile hydratase activity
B	0046914	molecular_function	transition metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 300

Chain	Residue
A	CYS109
A	CSD112
A	ALA113
A	CSO114
A	HOH502

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TAY B 300

Chain	Residue
B	ARG56
B	TYR72
B	TYR76
A	CSD112
A	CSO114
A	TRP117
B	MET40

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 57

Chain	Residue	Details
B	ARG56	electrostatic stabiliser, proton acceptor, proton donor
B	TYR72	proton acceptor, proton donor
B	TYR76	increase acidity, increase basicity
A	ILE119	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

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