4WZ5

Crystal structure of P. aeruginosa OXA10

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0008658	molecular_function	penicillin 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	0071555	biological_process	cell wall organization
B	0005886	cellular_component	plasma membrane
B	0008658	molecular_function	penicillin 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	0071555	biological_process	cell wall organization
C	0005886	cellular_component	plasma membrane
C	0008658	molecular_function	penicillin 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	0071555	biological_process	cell wall organization
D	0005886	cellular_component	plasma membrane
D	0008658	molecular_function	penicillin 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	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue SO4 A 301

Chain	Residue
A	ARG160

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 302

Chain	Residue
A	THR80
A	ARG131
A	LYS134
A	TYR135

---

site_id	AC3
Number of Residues	13
Details	binding site for residue 3VU A 303

Chain	Residue
A	VAL117
A	LEU155
A	GLY207
A	PHE208
A	SER209
A	ARG250
A	HOH416
A	HOH430
A	HOH459
A	ALA66
A	SER67
A	TRP102
A	SER115

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 B 301

Chain	Residue
B	THR80
B	ARG131
B	LYS134
B	TYR135

---

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 B 302

Chain	Residue
B	ARG160
B	HOH470

---

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 B 303

Chain	Residue
B	GLY128
B	GLU129
B	VAL130
B	HOH448

---

site_id	AC7
Number of Residues	14
Details	binding site for residue 3VU B 304

Chain	Residue
B	ALA66
B	SER67
B	TRP102
B	SER115
B	VAL117
B	LEU155
B	GLY207
B	PHE208
B	SER209
B	ARG250
B	HOH418
B	HOH436
B	HOH439
B	HOH451

---

site_id	AC8
Number of Residues	9
Details	binding site for residue SO4 C 301

Chain	Residue
B	LYS95
C	SER67
C	SER115
C	LYS205
C	THR206
C	GLY207
C	PHE208
C	ARG250
C	HOH452

---

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 C 302

Chain	Residue
C	TYR63
C	LEU64
C	VAL219
C	HOH472

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 C 303

Chain	Residue
C	SER181
C	LYS182
C	HOH457

---

site_id	AD2
Number of Residues	7
Details	binding site for residue SO4 C 304

Chain	Residue
A	THR107
A	ARG109
C	PRO198
C	GLU227
C	GLU229
C	HOH440
C	HOH464

---

site_id	AD3
Number of Residues	6
Details	binding site for residue CO2 C 305

Chain	Residue
C	SER67
C	LYS70
C	VAL117
C	PHE120
C	TRP154
C	LEU155

---

site_id	AD4
Number of Residues	9
Details	binding site for residue SO4 D 301

Chain	Residue
A	LYS95
D	SER67
D	SER115
D	LYS205
D	THR206
D	GLY207
D	PHE208
D	ARG250
D	HOH543

---

site_id	AD5
Number of Residues	9
Details	binding site for residue SO4 D 302

Chain	Residue
B	GLU199
B	TYR200
B	GLU227
B	GLU229
D	THR107
D	ARG109
D	GLY110
D	HOH460
D	HOH530

---

site_id	AD6
Number of Residues	8
Details	binding site for residue SO4 D 303

Chain	Residue
B	THR107
B	ARG109
D	PRO198
D	GLU199
D	TYR200
D	GLU227
D	GLU229
D	HOH448

---

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 D 304

Chain	Residue
D	LYS182
B	HOH477
D	SER181

---

site_id	AD8
Number of Residues	7
Details	binding site for residue CO2 D 305

Chain	Residue
D	SER67
D	LYS70
D	VAL117
D	PHE120
D	TRP154
D	LEU155
D	HOH442

---

Functional Information from PROSITE/UniProt

site_id	PS00337
Number of Residues	11
Details	BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI

Chain	Residue	Details
C	PRO65-ILE75
A	PRO65-ILE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11188693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RL3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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