6V1O

Structure of OXA-48 bound to QPX7728 at 1.80 A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008658	molecular_function	penicillin binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0008658	molecular_function	penicillin binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
C	0008658	molecular_function	penicillin binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
D	0008658	molecular_function	penicillin binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
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	13
Details	binding site for residue RM9 A 301

Chain	Residue
A	ALA69
A	TYR211
A	LEU247
A	ARG250
A	HOH522
A	SER70
A	KCX73
A	TRP105
A	SER118
A	VAL120
A	LYS208
A	THR209
A	GLY210

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	GLU37
A	GLU256
A	HOH403
A	HOH456
A	HOH576
A	HOH623

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 303

Chain	Residue
A	ASP143
A	GLU147
A	HOH471
A	HOH492
A	HOH499
A	HOH539

---

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 304

Chain	Residue
A	ARG206
A	HOH666
B	ARG206

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG B 302

Chain	Residue
B	ASP143
B	GLU147
B	HOH404
B	HOH438
B	HOH535
B	HOH537

---

site_id	AC6
Number of Residues	6
Details	binding site for residue MG B 303

Chain	Residue
B	GLU37
B	GLU256
B	HOH410
B	HOH479
B	HOH485
B	HOH591

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MG C 302

Chain	Residue
C	ASP143
C	GLU147
C	HOH414
C	HOH467
C	HOH515
C	HOH577

---

site_id	AC8
Number of Residues	2
Details	binding site for residue CL C 303

Chain	Residue
C	ARG206
D	ARG206

---

site_id	AC9
Number of Residues	6
Details	binding site for residue MG D 302

Chain	Residue
D	ASP143
D	GLU147
D	HOH436
D	HOH492
D	HOH520
D	HOH551

---

site_id	AD1
Number of Residues	5
Details	binding site for residue MG D 303

Chain	Residue
C	HOH437
C	HOH708
D	HOH422
D	HOH658
D	HOH704

---

site_id	AD2
Number of Residues	5
Details	binding site for residue MG D 304

Chain	Residue
D	HIS140
D	HOH501
D	HOH530
D	HOH564
D	HOH665

---

site_id	AD3
Number of Residues	15
Details	binding site for Di-peptide RM9 B 301 and SER B 70

Chain	Residue
B	PRO68
B	ALA69
B	THR71
B	PHE72
B	KCX73
B	TRP105
B	SER118
B	VAL120
B	LYS208
B	THR209
B	GLY210
B	TYR211
B	LEU247
B	ARG250
B	HOH482

---

site_id	AD4
Number of Residues	15
Details	binding site for Di-peptide RM9 C 301 and SER C 70

Chain	Residue
C	PRO68
C	ALA69
C	THR71
C	PHE72
C	KCX73
C	TRP105
C	SER118
C	VAL120
C	LYS208
C	THR209
C	GLY210
C	TYR211
C	LEU247
C	ARG250
C	HOH413

---

site_id	AD5
Number of Residues	14
Details	binding site for Di-peptide RM9 D 301 and SER D 70

Chain	Residue
D	TRP105
D	SER118
D	VAL120
D	LYS208
D	THR209
D	GLY210
D	TYR211
D	ARG250
D	HOH531
D	PRO68
D	ALA69
D	THR71
D	PHE72
D	KCX73

---

Functional Information from PROSITE/UniProt

site_id	PS00337
Number of Residues	11
Details	BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL

Chain	Residue	Details
A	PRO68-LEU78

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