Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1R44

Crystal Structure of VanX

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 203

Chain	Residue
A	HIS116
A	ASP123
A	HIS184
A	HOH205

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 203

Chain	Residue
B	HIS116
B	ASP123
B	HIS184
B	HOH204

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 203

Chain	Residue
C	ASP123
C	HIS184
C	HIS116

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 203

Chain	Residue
D	HIS116
D	ASP123
D	HIS184
D	HOH204

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 203

Chain	Residue
E	HIS116
E	ASP123
E	HIS184
E	HOH205

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 203

Chain	Residue
F	HIS116
F	ASP123
F	HIS184
F	HOH205

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:9702193

Chain	Residue	Details
A	GLU181
B	GLU181
C	GLU181
D	GLU181
E	GLU181
F	GLU181

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01924, ECO:0000269\|PubMed:9702193

Chain	Residue	Details
A	HIS116
D	HIS116
D	ASP123
D	HIS184
E	HIS116
E	ASP123
E	HIS184
F	HIS116
F	ASP123
F	HIS184
A	ASP123
A	HIS184
B	HIS116
B	ASP123
B	HIS184
C	HIS116
C	ASP123
C	HIS184

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000305

Chain	Residue	Details
A	ARG71
B	ARG71
C	ARG71
D	ARG71
E	ARG71
F	ARG71

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details

Chain	Residue	Details
A	GLU181
A	ARG71

site_id	CSA2
Number of Residues	2
Details

Chain	Residue	Details
B	GLU181
B	ARG71

site_id	CSA3
Number of Residues	2
Details

Chain	Residue	Details
C	GLU181
C	ARG71

site_id	CSA4
Number of Residues	2
Details

Chain	Residue	Details
D	GLU181
D	ARG71

site_id	CSA5
Number of Residues	2
Details

Chain	Residue	Details
E	GLU181
E	ARG71

site_id	CSA6
Number of Residues	2
Details

Chain	Residue	Details
F	GLU181
F	ARG71

site_id	MCSA1
Number of Residues	5
Details	M-CSA 706

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

site_id	MCSA2
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

site_id	MCSA3
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

site_id	MCSA4
Number of Residues	5
Details	M-CSA 706

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

site_id	MCSA5
Number of Residues	5
Details	M-CSA 706

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

site_id	MCSA6
Number of Residues	5
Details	M-CSA 706

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)