4WMC

OXA-48 covalent complex with Avibactam inhibitor

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
E	0005886	cellular_component	plasma membrane
E	0008658	molecular_function	penicillin binding
E	0008800	molecular_function	beta-lactamase activity
E	0016787	molecular_function	hydrolase activity
E	0017001	biological_process	antibiotic catabolic process
E	0046677	biological_process	response to antibiotic
E	0071555	biological_process	cell wall organization
F	0005886	cellular_component	plasma membrane
F	0008658	molecular_function	penicillin binding
F	0008800	molecular_function	beta-lactamase activity
F	0016787	molecular_function	hydrolase activity
F	0017001	biological_process	antibiotic catabolic process
F	0046677	biological_process	response to antibiotic
F	0071555	biological_process	cell wall organization
G	0005886	cellular_component	plasma membrane
G	0008658	molecular_function	penicillin binding
G	0008800	molecular_function	beta-lactamase activity
G	0016787	molecular_function	hydrolase activity
G	0017001	biological_process	antibiotic catabolic process
G	0046677	biological_process	response to antibiotic
G	0071555	biological_process	cell wall organization
H	0005886	cellular_component	plasma membrane
H	0008658	molecular_function	penicillin binding
H	0008800	molecular_function	beta-lactamase activity
H	0016787	molecular_function	hydrolase activity
H	0017001	biological_process	antibiotic catabolic process
H	0046677	biological_process	response to antibiotic
H	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue NXL A 301

Chain	Residue
A	SER70
A	HOH419
A	SER118
A	VAL120
A	LEU158
A	LYS208
A	THR209
A	GLY210
A	TYR211
A	ARG250

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CO2 A 302

Chain	Residue
A	LYS73
A	ASN76
A	TYR123
A	TRP157

---

site_id	AC3
Number of Residues	11
Details	binding site for residue NXL B 301

Chain	Residue
B	ALA69
B	SER70
B	SER118
B	VAL120
B	LEU158
B	LYS208
B	THR209
B	GLY210
B	TYR211
B	ARG250
B	HOH428

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CO2 C 302

Chain	Residue
C	LYS73
C	ASN76
C	TRP157
C	HOH410

---

site_id	AC5
Number of Residues	5
Details	binding site for residue CO2 F 302

Chain	Residue
F	SER70
F	LYS73
F	TYR123
F	TRP157
F	HOH417

---

site_id	AC6
Number of Residues	15
Details	binding site for Di-peptide NXL C 301 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	HOH410
C	HOH411

---

site_id	AC7
Number of Residues	13
Details	binding site for Di-peptide NXL D 301 and SER D 70

Chain	Residue
D	PRO68
D	ALA69
D	THR71
D	PHE72
D	KCX73
D	SER118
D	VAL120
D	LYS208
D	THR209
D	GLY210
D	TYR211
D	ARG250
D	HOH401

---

site_id	AC8
Number of Residues	16
Details	binding site for Di-peptide NXL E 301 and SER E 70

Chain	Residue
E	PRO68
E	ALA69
E	THR71
E	PHE72
E	KCX73
E	SER118
E	VAL120
E	LEU158
E	LYS208
E	THR209
E	GLY210
E	TYR211
E	THR213
E	ARG250
E	HOH428
E	HOH402

---

site_id	AC9
Number of Residues	15
Details	binding site for Di-peptide NXL F 301 and SER F 70

Chain	Residue
F	PRO68
F	ALA69
F	THR71
F	PHE72
F	LYS73
F	SER118
F	LEU158
F	LYS208
F	THR209
F	GLY210
F	TYR211
F	THR213
F	ARG250
F	CO2302
F	HOH417

---

site_id	AD1
Number of Residues	12
Details	binding site for Di-peptide NXL G 301 and SER G 70

Chain	Residue
G	LEU158
G	LYS208
G	THR209
G	GLY210
G	TYR211
G	ARG250
G	PRO68
G	ALA69
G	THR71
G	PHE72
G	LYS73
G	SER118

---

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

Chain	Residue
H	PRO68
H	ALA69
H	THR71
H	PHE72
H	LYS73
H	SER118
H	VAL120
H	LEU158
H	LYS208
H	THR209
H	GLY210
H	TYR211
H	ARG250
H	HOH420
H	HOH401

---

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
D	PRO68-LEU78
A	PRO68-LEU78

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26731698","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31358584","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32150407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P97","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P99","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V1O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19477418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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