4IBX

Crystal structure of stabilized TEM-1 beta-lactamase variant v.13

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA A 301

Chain	Residue
A	GLU37
A	ASP38
A	HOH425
B	GLU37
B	ASP38
B	HOH412
B	HOH415
B	HOH420

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MES A 302

Chain	Residue
A	VAL216
A	LYS234
A	SER235
A	GLY236
A	ALA237
A	ARG244
A	SER130

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MES B 301

Chain	Residue
B	TYR105
B	VAL216
B	SER235
B	GLY236
B	ALA237
B	ARG244

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 301

Chain	Residue
C	GLU37
C	ASP38
C	HOH407
E	GLU37
E	ASP38
E	HOH306

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	SER130
C	VAL216
C	SER235
C	GLY236
C	ALA237
C	ARG244
C	HOH411

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MES D 301

Chain	Residue
D	TYR105
D	SER130
D	VAL216
D	SER235
D	GLY236
D	ALA237
D	ARG244
D	HOH409

---

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	5
Details	ACT_SITE: Acyl-ester intermediate

Chain	Residue	Details
A	SER70
B	SER70
C	SER70
D	SER70
E	SER70

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	GLU168
B	GLU168
C	GLU168
D	GLU168
E	GLU168

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	LYS234
B	LYS234
C	LYS234
D	LYS234
E	LYS234

---

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	GLU166	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	GLU166	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	GLU166	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	GLU166	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	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	LYS234	electrostatic stabiliser
E	ALA237	electrostatic stabiliser, hydrogen bond donor

---