1WUO

Crystal structure of metallo-beta-lactamase IMP-1 mutant (D81A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion 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	0046872	molecular_function	metal ion binding
B	0008270	molecular_function	zinc ion 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	0046872	molecular_function	metal ion binding
C	0008270	molecular_function	zinc ion 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	0046872	molecular_function	metal ion binding
D	0008270	molecular_function	zinc ion 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	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS77
A	HIS79
A	HIS139
A	CSD158
A	ACY401

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	ACY402
B	HIS77
B	HIS79
B	HIS139
B	CSD158

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 303

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	CSD158
C	ACY403

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 304

Chain	Residue
D	HIS77
D	HIS79
D	HIS139
D	CSD158
D	ACY404

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY A 401

Chain	Residue
A	HIS77
A	HIS79
A	ALA81
A	HIS139
A	CSD158
A	ZN301
A	HOH438

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 402

Chain	Residue
B	HIS79
B	HIS139
B	CSD158
B	ZN302
B	HOH413

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY C 403

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	CSD158
C	ZN303
C	HOH404
C	HOH445

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY D 404

Chain	Residue
D	HIS77
D	HIS79
D	ALA81
D	HIS139
D	CSD158
D	ZN304
D	HOH405
D	HOH406

---

Functional Information from PROSITE/UniProt

site_id	PS00744
Number of Residues	13
Details	BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK

Chain	Residue	Details
A	PRO149-LYS161

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
A	ALA81

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
B	ALA81

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
C	ALA81

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1qh5

Chain	Residue	Details
D	ALA81

---