Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HP5

Crystal Structure of the OXA-10 W154G mutant at pH 7.0

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	7
Details	BINDING SITE FOR RESIDUE SO4 A 267

Chain	Residue
A	SER67
A	SER115
A	LYS205
A	THR206
A	GLY207
A	PHE208
A	ARG250

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 267

Chain	Residue
B	THR206
B	GLY207
B	PHE208
B	ARG250
B	SER67
B	SER115

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 267

Chain	Residue
C	SER67
C	SER115
C	LYS205
C	THR206
C	GLY207
C	PHE208
C	ARG250

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 267

Chain	Residue
D	SER115
D	THR206
D	GLY207
D	PHE208
D	ARG250

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 268

Chain	Residue
A	ARG104
B	THR80
B	ARG131
B	TYR135

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 268

Chain	Residue
A	THR80
A	ARG131
A	LYS134
A	TYR135

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 268

Chain	Residue
C	PRO248
C	ARG250
C	LYS251

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 268

Chain	Residue
D	THR80
D	ARG131
D	TYR135

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 269

Chain	Residue
D	PRO248
D	ARG250
D	LYS251

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 269

Chain	Residue
B	PRO248
B	ARG250
B	LYS251

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 269

Chain	Residue
A	LEU201
A	HIS203
A	GLU227
B	GLU190
B	HOH278

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 270

Chain	Residue
A	GLU190
A	HOH283
B	LEU201
B	HIS203
B	GLU227

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO D 270

Chain	Residue
C	GLU190
C	HOH270
D	HIS203
D	GLU227

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO C 269

Chain	Residue
C	HIS203
C	GLU227
C	HOH275
D	GLU190

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	4
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000269\|PubMed:11724923, ECO:0000269\|PubMed:19860471, ECO:0007744\|PDB:1K54, ECO:0007744\|PDB:2WGI

Chain	Residue	Details
A	SER67
B	SER67
C	SER67
D	SER67

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:19860471, ECO:0007744\|PDB:2WGI

Chain	Residue	Details
A	SER115
C	THR206
C	PHE208
C	ARG250
D	SER115
D	THR206
D	PHE208
D	ARG250
A	THR206
A	PHE208
A	ARG250
B	SER115
B	THR206
B	PHE208
B	ARG250
C	SER115

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:11188693, ECO:0000269\|PubMed:11724923, ECO:0000269\|PubMed:19860471, ECO:0007744\|PDB:1E4D, ECO:0007744\|PDB:1K4E, ECO:0007744\|PDB:1K4F, ECO:0007744\|PDB:1K54, ECO:0007744\|PDB:1K55, ECO:0007744\|PDB:1K56, ECO:0007744\|PDB:1K57, ECO:0007744\|PDB:1K6S, ECO:0007744\|PDB:2RL3

Chain	Residue	Details
A	LYS70
B	LYS70
C	LYS70
D	LYS70

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1m6k

Chain	Residue	Details
A	SER67

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1m6k

Chain	Residue	Details
B	SER67

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1m6k

Chain	Residue	Details
C	SER67

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1m6k

Chain	Residue	Details
D	SER67

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)