8XZ2

The structural model of a homodimeric D-Ala-D-Ala metallopeptidase, VanX, from vancomycin-resistant bacteria

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0016805	molecular_function	dipeptidase activity
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0016805	molecular_function	dipeptidase activity
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
C	0071555	biological_process	cell wall organization

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:9702193

Chain	Residue	Details
B	GLU181
C	GLU181

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9702193

Chain	Residue	Details
B	HIS116
B	ASP123
B	HIS184
C	HIS116
C	ASP123
C	HIS184

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305

Chain	Residue	Details
B	ARG71
C	ARG71

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 706

Chain	Residue	Details
B	ARG71	electrostatic stabiliser
B	HIS116	metal ligand
B	ASP123	metal ligand
B	GLU181	proton acceptor, proton donor
B	HIS184	metal ligand

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 706

Chain	Residue	Details
C	ARG71	electrostatic stabiliser
C	HIS116	metal ligand
C	ASP123	metal ligand
C	GLU181	proton acceptor, proton donor
C	HIS184	metal ligand

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