6PQI

Crystal Structure of Class D Beta-lactamase OXA-48 with Cefotaxime

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	13
Details	binding site for residue CEF A 301

Chain	Residue
A	SER70
A	THR213
A	ARG214
A	ARG250
A	HOH426
A	ILE102
A	TRP105
A	SER118
A	VAL120
A	THR209
A	GLY210
A	TYR211
A	SER212

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site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 302

Chain	Residue
A	ARG206
B	ARG206

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site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 303

Chain	Residue
A	LYS73
A	TRP157

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site_id	AC4
Number of Residues	1
Details	binding site for residue ACT A 304

Chain	Residue
A	ASP96

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

Chain	Residue
B	LYS73
B	VAL120
B	TRP157

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site_id	AC6
Number of Residues	2
Details	binding site for residue CL C 302

Chain	Residue
C	LYS73
C	TRP157

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site_id	AC7
Number of Residues	2
Details	binding site for residue ACT C 303

Chain	Residue
C	ASP96
C	PRO121

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site_id	AC8
Number of Residues	1
Details	binding site for residue CL D 302

Chain	Residue
D	ARG206

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site_id	AC9
Number of Residues	3
Details	binding site for residue CL D 303

Chain	Residue
D	LYS73
D	TRP157
D	HOH439

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site_id	AD1
Number of Residues	3
Details	binding site for residue ACT D 304

Chain	Residue
D	LYS94
D	TRP95
D	ASP96

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site_id	AD2
Number of Residues	15
Details	binding site for Di-peptide CEF B 301 and SER B 70

Chain	Residue
B	PRO68
B	ALA69
B	THR71
B	PHE72
B	LYS73
B	TRP105
B	SER118
B	VAL120
B	LEU158
B	LYS208
B	THR209
B	GLY210
B	TYR211
B	THR213
B	ARG250

---

site_id	AD3
Number of Residues	14
Details	binding site for Di-peptide CEF C 301 and SER C 70

Chain	Residue
C	PRO68
C	ALA69
C	THR71
C	PHE72
C	LYS73
C	SER118
C	VAL120
C	LYS208
C	THR209
C	GLY210
C	TYR211
C	SER212
C	THR213
C	ARG250

---

site_id	AD4
Number of Residues	14
Details	binding site for Di-peptide CEF D 301 and SER D 70

Chain	Residue
D	PRO68
D	ALA69
D	THR71
D	PHE72
D	LYS73
D	TRP105
D	SER118
D	VAL120
D	LYS208
D	THR209
D	GLY210
D	TYR211
D	THR213
D	ARG250

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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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