Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M2X

Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril

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	4
Details	BINDING SITE FOR RESIDUE NA A 302

Chain	Residue
A	ASN150
A	LYS167
A	ARG169
D	LYS148

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 901

Chain	Residue
A	HIS116
A	HIS118
A	HIS196
A	MCO811
A	ZN902

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 902

Chain	Residue
A	ASP120
A	CYS221
A	HIS263
A	MCO811
A	ZN901

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 901

Chain	Residue
B	HIS116
B	HIS118
B	HIS196
B	MCO812
B	ZN902

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 902

Chain	Residue
B	ASP120
B	CYS221
B	HIS263
B	MCO812
B	ZN901

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 901

Chain	Residue
C	HIS116
C	HIS118
C	HIS196
C	MCO813
C	ZN902

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 902

Chain	Residue
C	ASP120
C	CYS221
C	HIS263
C	MCO813
C	ZN901

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 901

Chain	Residue
D	HIS116
D	HIS118
D	HIS196
D	MCO814
D	ZN902

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 902

Chain	Residue
D	ASP120
D	CYS221
D	HIS263
D	MCO814
D	ZN901

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 900

Chain	Residue
A	HIS285
A	ASP288
A	HOH1084
A	HOH1085
A	HOH1086

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 900

Chain	Residue
A	HOH1087
B	HIS285
B	ASP288
B	HOH1070
B	HOH1071

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 900

Chain	Residue
C	HIS285
C	ASP288
C	HOH1074
C	HOH1075
D	HOH1089

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 900

Chain	Residue
D	HIS285
D	ASP288
D	HOH1090
D	HOH1091
D	HOH1092

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MCO A 811

Chain	Residue
A	TYR100
A	HIS118
A	ASP119
A	ASP120
A	LYS167
A	HIS196
A	TYR233
A	ZN901
A	ZN902
A	HOH985
A	HOH996
A	HOH1073

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MCO B 812

Chain	Residue
B	HIS118
B	ASP119
B	ASP120
B	LYS167
B	HIS196
B	TYR233
B	ZN901
B	ZN902
B	HOH1012
B	HOH1049
B	HOH1069
D	TYR100

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MCO C 813

Chain	Residue
B	TYR100
C	HIS118
C	ASP119
C	ASP120
C	LYS167
C	HIS196
C	TYR233
C	ZN901
C	ZN902
C	HOH1010
C	HOH1048

site_id	BC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MCO D 814

Chain	Residue
C	TYR100
D	HIS118
D	ASP119
D	ASP120
D	LYS167
D	HIS196
D	TYR233
D	ZN901
D	ZN902
D	HOH977
D	HOH1034

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 801

Chain	Residue
A	GLY235
A	GLU236
A	ALA237
A	TYR238
A	HOH950
A	HOH1023
B	GLN171

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 802

Chain	Residue
B	GLY235
B	GLU236
B	ALA237
B	HOH933
B	HOH1025

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 803

Chain	Residue
C	GLN171
C	GLY235
C	GLU236
C	ALA237
C	HOH970
C	HOH1006

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 804

Chain	Residue
A	GLN171
D	GLY235
D	GLU236
D	ALA237
D	TYR238
D	HOH1030

Functional Information from PROSITE/UniProt

site_id	PS00743
Number of Residues	20
Details	BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IaTHsHDDraGGleyfgki.G

Chain	Residue	Details
A	ILE113-GLY133

site_id	PS00744
Number of Residues	13
Details	BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkekVLvGgCIIK

Chain	Residue	Details
A	PRO209-LYS224

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12684522","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP120

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

Chain	Residue	Details
B	ASP120

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

Chain	Residue	Details
C	ASP120

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

Chain	Residue	Details
D	ASP120

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