6PSG

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
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	0071555	biological_process	cell wall organization
B	0005886	cellular_component	plasma membrane
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	0071555	biological_process	cell wall organization
C	0005886	cellular_component	plasma membrane
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	0071555	biological_process	cell wall organization
D	0005886	cellular_component	plasma membrane
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	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 301

Chain	Residue
A	ARG206
B	ARG206

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site_id	AC2
Number of Residues	9
Details	binding site for residue DGF A 302

Chain	Residue
A	TYR211
A	ARG250
A	ALA69
A	SER70
A	SER118
A	VAL120
A	LEU158
A	THR209
A	GLY210

---

site_id	AC3
Number of Residues	2
Details	binding site for residue CL C 301

Chain	Residue
C	ARG206
D	ARG206

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site_id	AC4
Number of Residues	5
Details	binding site for residue GOL C 303

Chain	Residue
C	LYS94
C	TRP95
C	ASP96
C	GLU125
C	HOH435

---

site_id	AC5
Number of Residues	15
Details	binding site for Di-peptide DGF 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	ARG250
B	HOH431

---

site_id	AC6
Number of Residues	14
Details	binding site for Di-peptide DGF C 302 and SER C 70

Chain	Residue
C	PRO68
C	ALA69
C	THR71
C	PHE72
C	LYS73
C	SER118
C	VAL120
C	LEU158
C	LYS208
C	THR209
C	GLY210
C	TYR211
C	ARG250
C	HOH462

---

site_id	AC7
Number of Residues	13
Details	binding site for Di-peptide DGF 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	ARG250

---

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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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:25406838, ECO:0000269|PubMed:26731698, ECO:0000269|PubMed:31358584, ECO:0000269|PubMed:32150407, ECO:0007744|PDB:4WMC, ECO:0007744|PDB:5FAQ, ECO:0007744|PDB:5FAS, ECO:0007744|PDB:6P97, ECO:0007744|PDB:6P98, ECO:0007744|PDB:6P99, ECO:0007744|PDB:6P9C, ECO:0007744|PDB:6V1O

Chain	Residue	Details
A	SER70
B	SER70
C	SER70
D	SER70

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q8RLA6

Chain	Residue	Details
A	SER70
D	SER70
D	SER118
D	ARG250
A	SER118
A	ARG250
B	SER70
B	SER118
B	ARG250
C	SER70
C	SER118
C	ARG250

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P13661

Chain	Residue	Details
A	LYS73
B	LYS73
C	LYS73
D	LYS73

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:19477418, ECO:0000269|PubMed:25406838, ECO:0007744|PDB:3HBR, ECO:0007744|PDB:4WMC

Chain	Residue	Details
A	LYS73
B	LYS73
C	LYS73
D	LYS73

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