Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E4D

Structure of OXA10 beta-lactamase at pH 8.3

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0046677	biological_process	response to antibiotic
A	0071555	biological_process	cell wall organization
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	0046677	biological_process	response to antibiotic
B	0071555	biological_process	cell wall organization
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	0046677	biological_process	response to antibiotic
C	0071555	biological_process	cell wall organization
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	0046677	biological_process	response to antibiotic
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 901

Chain	Residue
A	SER67
A	HOH2220
A	HOH2221
A	SER115
A	LYS205
A	THR206
A	GLY207
A	PHE208
A	ARG250
A	HOH2177
A	HOH2219

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 902

Chain	Residue
A	THR80
A	ARG131
A	LYS134
A	TYR135

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 903

Chain	Residue
A	MET99
A	LYS100
A	GLN101

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 904

Chain	Residue
A	GLY128
A	GLU129
A	VAL130
A	HOH2222
A	HOH2224
A	HOH2225

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 901

Chain	Residue
B	ASN85
B	HOH2243
B	HOH2244
D	ASN176
D	LYS182
D	HOH2171

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 902

Chain	Residue
B	PRO198
B	GLU199
B	GLU227
B	GLU229
B	HOH2245
B	HOH2246
D	THR107
D	ARG109

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 903

Chain	Residue
B	SER67
B	SER115
B	LYS205
B	THR206
B	GLY207
B	PHE208
B	ARG250
B	HOH2198
B	HOH2247

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 904

Chain	Residue
B	ARG160

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 905

Chain	Residue
B	THR80
B	ARG131
B	LYS134
B	TYR135

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 901

Chain	Residue
C	GLU195
C	TYR200
C	VAL202
C	TRP222
C	VAL226
C	THR255
C	MET258
C	HOH2164
C	HOH2214

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 902

Chain	Residue
C	THR206
C	LEU247
C	PRO248
C	ARG250
C	LYS251
C	HOH2215

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 903

Chain	Residue
B	HOH2101
B	HOH2105
C	MET99
C	LYS100
C	GLN101
C	HOH2216

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 C 904

Chain	Residue
C	SER67
C	SER115
C	LYS205
C	THR206
C	GLY207
C	PHE208
C	ARG250
C	HOH2092
C	HOH2217
C	HOH2218

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 901

Chain	Residue
A	LYS95
D	SER67
D	SER115
D	LYS205
D	THR206
D	GLY207
D	PHE208
D	ARG250
D	HOH2246

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 902

Chain	Residue
D	THR206
D	LEU247
D	PRO248
D	ARG250
D	LYS251

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 903

Chain	Residue
D	LYS182
D	HOH2247
D	HOH2248
B	GLU183
D	SER181

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 911

Chain	Residue
A	GLU195
A	TYR200
A	VAL202
A	MET258
A	GLU259
A	ILE263
A	HOH2217

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 911

Chain	Residue
B	GLU195
B	TYR200
B	GLU259
B	ILE263
B	HOH2185
B	HOH2249

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 912

Chain	Residue
B	ASN38
B	PRO217
B	ASP240
B	HOH2027
B	HOH2222
B	HOH2250

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 911

Chain	Residue
A	THR107
A	ARG109
C	PRO198
C	GLU199
C	TYR200
C	GLU229
C	HOH2219

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 911

Chain	Residue
D	GLN113
D	SER204
D	LYS205
D	THR206
D	HOH2198
D	HOH2249

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 912

Chain	Residue
D	GLU195
D	THR255
D	HOH2196

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

Chain	Residue	Details
A	SER67
B	SER67
C	SER67
D	SER67

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS205
B	LYS205
C	LYS205
D	LYS205

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:11188693

Chain	Residue	Details
A	KCX70
B	KCX70
C	KCX70
D	KCX70

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