Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RX2

A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030655	biological_process	beta-lactam antibiotic catabolic process
A	0046677	biological_process	response to antibiotic
B	0005515	molecular_function	protein binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030655	biological_process	beta-lactam antibiotic catabolic process
B	0046677	biological_process	response to antibiotic
C	0005515	molecular_function	protein binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0030655	biological_process	beta-lactam antibiotic catabolic process
C	0046677	biological_process	response to antibiotic
D	0005515	molecular_function	protein binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0030655	biological_process	beta-lactam antibiotic catabolic process
D	0046677	biological_process	response to antibiotic
E	0005515	molecular_function	protein binding
E	0008800	molecular_function	beta-lactamase activity
E	0016787	molecular_function	hydrolase activity
E	0017001	biological_process	antibiotic catabolic process
E	0030655	biological_process	beta-lactam antibiotic catabolic process
E	0046677	biological_process	response to antibiotic
F	0005515	molecular_function	protein binding
F	0008800	molecular_function	beta-lactamase activity
F	0016787	molecular_function	hydrolase activity
F	0017001	biological_process	antibiotic catabolic process
F	0030655	biological_process	beta-lactam antibiotic catabolic process
F	0046677	biological_process	response to antibiotic
G	0005515	molecular_function	protein binding
G	0008800	molecular_function	beta-lactamase activity
G	0016787	molecular_function	hydrolase activity
G	0017001	biological_process	antibiotic catabolic process
G	0030655	biological_process	beta-lactam antibiotic catabolic process
G	0046677	biological_process	response to antibiotic
H	0005515	molecular_function	protein binding
H	0008800	molecular_function	beta-lactamase activity
H	0016787	molecular_function	hydrolase activity
H	0017001	biological_process	antibiotic catabolic process
H	0030655	biological_process	beta-lactam antibiotic catabolic process
H	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	SER70
A	HOH458
A	HOH477
A	SER130
A	VAL216
A	LYS234
A	SER235
A	GLY236
A	ARG244
A	HOH421
A	HOH453

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	SER70
B	SER130
B	VAL216
B	LYS234
B	SER235
B	GLY236
B	ALA237
B	ARG244
B	HOH461

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	SER130
C	LYS234
C	SER235
C	GLY236
C	ALA237
C	ARG244
C	HOH424
C	HOH497

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 301

Chain	Residue
D	SER70
D	SER130
D	VAL216
D	LYS234
D	SER235
D	GLY236
D	ARG244

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 301

Chain	Residue
E	SER70
E	SER130
E	LYS234
E	SER235
E	GLY236
E	ALA237
E	ARG244

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 F 301

Chain	Residue
F	SER70
F	SER130
F	LYS234
F	SER235
F	GLY236
F	ALA237
F	ARG244
F	HOH416
F	HOH434
F	HOH472
F	HOH488

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 G 301

Chain	Residue
G	SER70
G	SER130
G	LYS234
G	SER235
G	GLY236
G	ARG244
G	HOH456

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 H 301

Chain	Residue
H	SER70
H	SER130
H	VAL216
H	LYS234
H	SER235
H	GLY236
H	ALA237
H	ARG244

Functional Information from PROSITE/UniProt

site_id	PS00146
Number of Residues	16
Details	BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL

Chain	Residue	Details
A	PHE66-LEU81

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Acyl-ester intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
A	SER70	electrostatic stabiliser
A	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS234	electrostatic stabiliser
A	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
B	SER70	electrostatic stabiliser
B	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS234	electrostatic stabiliser
B	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
C	SER70	electrostatic stabiliser
C	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	LYS234	electrostatic stabiliser
C	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
D	SER70	electrostatic stabiliser
D	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	LYS234	electrostatic stabiliser
D	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA5
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
E	SER70	electrostatic stabiliser
E	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	LYS234	electrostatic stabiliser
E	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA6
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
F	SER70	electrostatic stabiliser
F	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	LYS234	electrostatic stabiliser
F	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA7
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
G	SER70	electrostatic stabiliser
G	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	LYS234	electrostatic stabiliser
G	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA8
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
H	SER70	electrostatic stabiliser
H	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	TYR166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	LYS234	electrostatic stabiliser
H	ALA237	electrostatic stabiliser, hydrogen bond donor

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