1I5Q

CRYSTAL STRUCTURE OF THE E. COLI AMPC BETA-LACTAMASE MUTANT N152A COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, MOXALACTAM

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	15
Details	BINDING SITE FOR RESIDUE MOX A 964

Chain	Residue
A	SER64
A	ALA318
A	THR319
A	GLY320
A	ASN346
A	HOH576
A	HOH786
A	LYS67
A	LEU119
A	GLN120
A	TYR150
A	TYR221
A	LYS315
A	THR316
A	GLY317

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MOX B 964

Chain	Residue
B	SER64
B	LYS67
B	GLN120
B	TYR150
B	TYR221
B	ASN289
B	LYS315
B	THR316
B	GLY317
B	ALA318
B	THR319
B	GLY320
B	ASN346
B	HOH475
B	HOH476
B	HOH526
B	HOH658
B	HOH742

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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	PHE60-LYS67

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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:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x

Chain	Residue	Details
A	SER64
B	SER64

---

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	SER64
B	SER64

---

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	GLN120
B	GLN120

---

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

Chain	Residue	Details
A	TYR150
B	TYR150

---

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	ALA152
A	ALA318
B	ALA152
B	ALA318

---

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

Chain	Residue	Details
A	ASN343
B	ASN343

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Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU272
A	SER64
A	LYS315
A	TYR150
A	LYS67

---

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

Chain	Residue	Details
B	GLU272
B	SER64
B	LYS315
B	TYR150
B	LYS67

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