1FCN

Crystal Structure of the E. Coli AMPC Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Substrate Beta-Lactam LORACARBEF

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LOR A 961

Chain	Residue
A	SER61
A	HOH1003
A	HOH1015
B	ALA1
B	GLN3
A	LEU116
A	LEU117
A	ASN149
A	TYR218
A	GLY314
A	ALA315
A	ASN340
A	HOH1002

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LOR B 961

Chain	Residue
B	SER61
B	LEU116
B	ASN149
B	TYR218
B	ASN286
B	GLY314
B	ALA315
B	THR316
B	ASN340
B	HOH1012
B	HOH1013
B	HOH1022
B	HOH1028

---

Functional Information from PROSITE/UniProt

site_id	PS00336
Number of Residues	8
Details	BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK

Chain	Residue	Details
A	PHE57-LYS64

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:35486701, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x

Chain	Residue	Details
A	SER61
B	SER61

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	SER61
B	SER61

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9

Chain	Residue	Details
A	LEU117
B	LEU117

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	GLU147
B	GLU147

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	ASN149
A	ALA315
B	ASN149
B	ALA315

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM

Chain	Residue	Details
A	ASN340
B	ASN340

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1xx2

Chain	Residue	Details
A	SER61
A	LYS64
A	GLU269
A	GLU147
A	LYS312

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1xx2

Chain	Residue	Details
B	SER61
B	LYS64
B	GLU269
B	GLU147
B	LYS312

---