6U0Y

Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0017001	biological_process	antibiotic catabolic process
B	0008270	molecular_function	zinc ion binding
B	0008800	molecular_function	beta-lactamase activity
B	0017001	biological_process	antibiotic catabolic process
C	0008270	molecular_function	zinc ion binding
C	0008800	molecular_function	beta-lactamase activity
C	0017001	biological_process	antibiotic catabolic process
D	0008270	molecular_function	zinc ion binding
D	0008800	molecular_function	beta-lactamase activity
D	0017001	biological_process	antibiotic catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS105
A	HIS107
A	HIS181
A	ZN302
A	EDO305

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 302

Chain	Residue
A	EDO305
A	ASP109
A	HIS110
A	HIS246
A	ZN301

---

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO A 303

Chain	Residue
A	ARG137
A	ASN141
A	HOH508
A	HOH540
C	ALA156
C	ASP157
C	HOH493

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 304

Chain	Residue
A	ALA172
A	THR191
A	HOH433
A	HOH449

---

site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 305

Chain	Residue
A	TYR32
A	HIS105
A	HIS107
A	ASP109
A	PHE145
A	HIS181
A	ZN301
A	ZN302

---

site_id	AC6
Number of Residues	7
Details	binding site for residue ZN B 300

Chain	Residue
B	HIS105
B	HIS107
B	HIS181
B	ZN301
B	EDO302
B	HOH402
B	HOH468

---

site_id	AC7
Number of Residues	7
Details	binding site for residue ZN B 301

Chain	Residue
B	ASP109
B	HIS110
B	HIS246
B	ZN300
B	EDO302
B	HOH402
B	HOH468

---

site_id	AC8
Number of Residues	8
Details	binding site for residue EDO B 302

Chain	Residue
B	HIS107
B	ASP109
B	HIS181
B	HIS246
B	ZN300
B	ZN301
B	HOH402
B	HOH468

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 303

Chain	Residue
B	ARG158
B	VAL165
B	VAL166
B	THR167
B	HOH452

---

site_id	AD1
Number of Residues	7
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS105
C	HIS107
C	HIS181
C	ZN302
C	HOH406
C	HOH560
C	HOH568

---

site_id	AD2
Number of Residues	7
Details	binding site for residue ZN C 302

Chain	Residue
C	ASP109
C	HIS110
C	HIS246
C	ZN301
C	HOH406
C	HOH560
C	HOH562

---

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO C 303

Chain	Residue
C	CYS239
C	CYS267
C	HOH441
C	HOH510
C	HOH512

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO C 304

Chain	Residue
C	LEU90
C	ARG91
C	HOH424

---

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO C 305

Chain	Residue
C	LEU265
C	THR266
C	ALA269
C	HOH515
C	HOH539

---

site_id	AD6
Number of Residues	5
Details	binding site for residue ZN D 300

Chain	Residue
D	HIS105
D	HIS107
D	HIS181
D	ZN301
D	EDO302

---

site_id	AD7
Number of Residues	5
Details	binding site for residue ZN D 301

Chain	Residue
D	ASP109
D	HIS110
D	HIS246
D	ZN300
D	EDO302

---

site_id	AD8
Number of Residues	7
Details	binding site for residue EDO D 302

Chain	Residue
D	ZN301
D	HIS105
D	HIS107
D	ASP109
D	PHE145
D	HIS181
D	ZN300

---

Functional Information from PROSITE/UniProt

site_id	PS00743
Number of Residues	21
Details	BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG

Chain	Residue	Details
A	LEU102-GLY122

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