Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QIN

Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0008270	molecular_function	zinc ion binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
C	0008270	molecular_function	zinc ion binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0042597	cellular_component	periplasmic space
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
D	0008270	molecular_function	zinc ion binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0042597	cellular_component	periplasmic space
D	0046677	biological_process	response to antibiotic
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 2001

Chain	Residue
A	CYS120
A	HIS121
A	HIS263
A	ZN2002
A	HOH2192
A	HOH2313

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 2002

Chain	Residue
A	ZN2001
A	HOH2192
A	HOH2313
A	HIS116
A	HIS118
A	HIS196

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 2001

Chain	Residue
B	CYS120
B	HIS121
B	HIS263
B	ZN2002
B	HOH4232

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 2002

Chain	Residue
B	HIS116
B	HIS118
B	HIS196
B	ZN2001
B	HOH4232
B	HOH4241

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 2001

Chain	Residue
C	CYS120
C	HIS121
C	HIS263
C	ZN2002
C	HOH2241

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 2002

Chain	Residue
C	HIS116
C	HIS118
C	HIS196
C	ZN2001
C	HOH2241
C	HOH2252

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 2001

Chain	Residue
D	CYS120
D	HIS121
D	HIS263
D	ZN2002
D	HOH4261

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 2002

Chain	Residue
D	HIS116
D	HIS118
D	HIS196
D	ZN2001
D	HOH4261
D	HOH4347

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 3001

Chain	Residue
B	HIS51
B	HOH4240
D	HIS51
D	HOH4263

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 4001

Chain	Residue
D	HOH4031
D	HOH4120
D	HOH4130
D	HOH4242
D	HOH4259
D	HOH4366

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 4002

Chain	Residue
B	HOH4046
B	HOH4068
B	HOH4090
B	HOH4098
B	HOH4110
B	HOH4350

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:17999929, ECO:0000269\|PubMed:9811546

Chain	Residue	Details
A	HIS116
B	HIS196
C	HIS116
C	HIS118
C	CYS120
C	HIS121
C	HIS196
D	HIS116
D	HIS118
D	CYS120
D	HIS121
A	HIS118
D	HIS196
A	CYS120
A	HIS121
A	HIS196
B	HIS116
B	HIS118
B	CYS120
B	HIS121

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P25910

Chain	Residue	Details
A	ASP220
B	ASP220
C	ASP220
D	ASP220

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:9811546

Chain	Residue	Details
A	HIS263
B	HIS263
C	HIS263
D	HIS263

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
A	CYS120

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
B	CYS120

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
C	CYS120

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
D	CYS120

site_id	MCSA1
Number of Residues	7
Details	M-CSA 258

Chain	Residue	Details
A	HIS116	metal ligand
A	HIS118	metal ligand
A	CYS120	metal ligand
A	HIS121	metal ligand
A	HIS196	metal ligand
A	TYR228	electrostatic stabiliser, hydrogen bond donor
A	HIS263	metal ligand

site_id	MCSA2
Number of Residues	7
Details	M-CSA 258

Chain	Residue	Details
B	HIS116	metal ligand
B	HIS118	metal ligand
B	CYS120	metal ligand
B	HIS121	metal ligand
B	HIS196	metal ligand
B	TYR228	electrostatic stabiliser, hydrogen bond donor
B	HIS263	metal ligand

site_id	MCSA3
Number of Residues	7
Details	M-CSA 258

Chain	Residue	Details
C	HIS116	metal ligand
C	HIS118	metal ligand
C	CYS120	metal ligand
C	HIS121	metal ligand
C	HIS196	metal ligand
C	TYR228	electrostatic stabiliser, hydrogen bond donor
C	HIS263	metal ligand

site_id	MCSA4
Number of Residues	7
Details	M-CSA 258

Chain	Residue	Details
D	HIS116	metal ligand
D	HIS118	metal ligand
D	CYS120	metal ligand
D	HIS121	metal ligand
D	HIS196	metal ligand
D	TYR228	electrostatic stabiliser, hydrogen bond donor
D	HIS263	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)