5QAV

OXA-48 IN COMPLEX WITH COMPOUND 26b

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
A	0071555	biological_process	cell wall organization
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
B	0071555	biological_process	cell wall organization
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
C	0071555	biological_process	cell wall organization
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
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue EDO A 301

Chain	Residue
A	THR167
A	ILE170
A	SER171
A	ARG174
A	HOH531

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site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 302

Chain	Residue
A	HOH533
A	LYS94
A	TRP95
A	ASP96
A	HOH465

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site_id	AC3
Number of Residues	4
Details	binding site for residue EDO B 301

Chain	Residue
B	TYR177
B	GLU227
B	HOH464
B	HOH474

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site_id	AC4
Number of Residues	9
Details	binding site for residue L43 C 301

Chain	Residue
C	TRP105
C	LEU158
C	TYR211
C	ARG214
C	ARG250
C	HOH402
C	HOH412
C	HOH457
C	HOH523

---

site_id	AC5
Number of Residues	3
Details	binding site for residue CL C 302

Chain	Residue
A	ARG206
C	ARG206
C	HOH582

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site_id	AC6
Number of Residues	5
Details	binding site for residue EDO C 303

Chain	Residue
C	LYS94
C	TRP95
C	ASP96
C	HOH465
C	HOH563

---

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO C 304

Chain	Residue
A	HIS90
A	HOH452
C	TYR177
C	GLU227
C	VAL232
C	HOH421
C	HOH498

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site_id	AC8
Number of Residues	4
Details	binding site for residue EDO C 305

Chain	Residue
A	ASN200
A	ASP229
C	LYS116
C	HOH408

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site_id	AC9
Number of Residues	10
Details	binding site for residue L43 D 301

Chain	Residue
D	TRP105
D	LEU158
D	TYR211
D	ARG214
D	ARG250
D	HOH404
D	HOH411
D	HOH417
D	HOH518
D	HOH552

---

site_id	AD1
Number of Residues	1
Details	binding site for residue CL D 302

Chain	Residue
D	ARG206

---

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO D 303

Chain	Residue
D	ILE170
D	SER171
D	ARG174

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO D 304

Chain	Residue
D	TYR177
D	GLU227
D	VAL232
D	HOH410
D	HOH478
D	HOH483

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO D 305

Chain	Residue
D	LYS116
D	HOH433
D	HOH553

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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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