1O07

Crystal Structure of the complex between Q120L/Y150E mutant of AmpC and a beta-lactam inhibitor (MXG)

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	5
Details	BINDING SITE FOR RESIDUE K B 1

Chain	Residue
B	GLY214
B	ASP217
B	HOH445
B	HOH475
B	HOH559

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 2

Chain	Residue
A	GLY214
A	ASP217
A	HOH470

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MXG A 400

Chain	Residue
A	LEU119
A	GLU150
A	ASN152
A	ARG204
A	VAL211
A	SER212
A	TYR221
A	ASP288
A	ALA292
A	ALA318
A	GLY320
A	ASN343
A	HOH744
A	HOH794
A	HOH795
A	HOH797
A	HOH798
B	HOH697
A	SER64

---

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE MXG B 400

Chain	Residue
B	GLY63
B	SER64
B	LEU119
B	ASN152
B	ARG204
B	VAL209
B	VAL211
B	SER212
B	TYR221
B	ASN289
B	LEU293
B	ALA318
B	THR319
B	GLY320
B	ASN343
B	ASN346
B	HOH538
B	HOH572
B	HOH608
B	HOH609
B	HOH750
B	HOH753
B	HOH766
B	HOH806
B	HOH807

---

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:35486701, 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	LEU120
B	LEU120

---

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

Chain	Residue	Details
A	GLU150
B	GLU150

---

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	ASN152
A	ALA318
B	ASN152
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

---

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	GLU150
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	GLU150
B	LYS67

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