3LCE

Crystal Structure of Oxa-10 Beta-Lactamase Covalently Bound to Cyclobutanone Beta-Lactam Mimic

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	0042597	cellular_component	periplasmic space
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	0042597	cellular_component	periplasmic space
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	0042597	cellular_component	periplasmic space
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	0042597	cellular_component	periplasmic space
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	5
Details	BINDING SITE FOR RESIDUE GOL A 1

Chain	Residue
A	THR80
A	ARG131
A	LYS134
A	TYR135
A	HOH854

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 267

Chain	Residue
A	THR206
A	ARG250
A	LYS251
A	LCE269

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 268

Chain	Residue
A	ALA197
A	PRO198
A	GLU199
A	TYR200
A	GLU229
A	HOH284
C	THR107
C	ARG109

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LCE A 269

Chain	Residue
A	ALA66
A	SER67
A	KCX70
A	SER115
A	VAL117
A	LEU155
A	THR206
A	GLY207
A	PHE208
A	ARG250
A	GOL267
A	HOH334

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
B	ARG160
B	HOH638

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 267

Chain	Residue
B	ARG131
B	LYS134
B	TYR135

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 268

Chain	Residue
B	ALA197
B	PRO198
B	GLU199
B	TYR200
B	GLU229
B	HOH407
D	THR107
D	ARG109

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 269

Chain	Residue
B	SER181
B	LYS182
B	HOH609

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LCE B 270

Chain	Residue
B	ALA66
B	SER67
B	KCX70
B	SER115
B	VAL117
B	THR206
B	GLY207
B	PHE208
B	ARG250

---

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 1

Chain	Residue
B	LYS95
C	SER67
C	SER115
C	LYS205
C	THR206
C	GLY207
C	PHE208
C	ARG250
C	HOH280
C	HOH291
C	HOH294

---

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 267

Chain	Residue
A	THR107
A	ARG109
C	HOH7
C	ALA197
C	PRO198
C	GLU199
C	TYR200
C	GLU227
C	GLU229
C	HOH336

---

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 D 2

Chain	Residue
A	LYS95
D	SER67
D	SER115
D	LYS205
D	THR206
D	GLY207
D	PHE208
D	ARG250
D	HOH286
D	HOH758
D	HOH834

---

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL D 1

Chain	Residue
D	HOH844

---

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 267

Chain	Residue
B	HOH13
B	THR107
B	ARG109
D	ALA197
D	PRO198
D	GLU199
D	TYR200
D	GLU227
D	GLU229
D	HOH305

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 268

Chain	Residue
D	GLN158
D	HOH620
D	ASN145
D	SER147

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO65-ILE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11188693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RL3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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