5MMY

Crystal structure of OXA10 with HEPES

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue EPE A 301

Chain	Residue
A	SER67
A	HOH415
A	HOH428
A	HOH486
A	MET99
A	SER115
A	GLU129
A	THR206
A	GLY207
A	PHE208
A	SER209
A	ARG250

---

site_id	AC2
Number of Residues	7
Details	binding site for residue DMS A 302

Chain	Residue
A	THR107
A	ARG109
A	HOH524
B	PRO198
B	GLU199
B	GLU227
B	GLU229

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 303

Chain	Residue
A	LYS138
A	PHE139
A	SER140
A	GLU168
A	SER172
A	HOH500

---

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 304

Chain	Residue
A	GLU79
A	ARG131
A	LYS134
A	TYR135
A	LYS152
A	GLU156

---

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

Chain	Residue
A	ALA98
A	ILE146
A	SER147
A	GLY148
A	GLY149
A	ILE150
A	HOH404
A	HOH541

---

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL A 306

Chain	Residue
A	ALA197
A	PRO198
A	GLU199
A	TYR200
A	GLU227
A	GLU229
B	THR107
B	ARG109

---

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 307

Chain	Residue
A	THR80
A	ARG131
A	HOH487

---

site_id	AC8
Number of Residues	5
Details	binding site for residue CL A 308

Chain	Residue
A	ARG97
A	ALA98
A	PRO118
A	HOH510
A	HOH585

---

site_id	AC9
Number of Residues	4
Details	binding site for residue CO3 B 301

Chain	Residue
B	SER67
B	SER115
B	THR206
B	ARG250

---

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
A	PRO65-ILE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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	8
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	2
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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