Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OVG

The crystal structure of an amidohydrolase from Mycoplasma synoviae with Zn ion bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0009056	biological_process	catabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0050490	molecular_function	1,4-lactonase activity
B	0008270	molecular_function	zinc ion binding
B	0009056	biological_process	catabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0050490	molecular_function	1,4-lactonase activity
C	0008270	molecular_function	zinc ion binding
C	0009056	biological_process	catabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0050490	molecular_function	1,4-lactonase activity
D	0008270	molecular_function	zinc ion binding
D	0009056	biological_process	catabolic process
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0050490	molecular_function	1,4-lactonase activity
E	0008270	molecular_function	zinc ion binding
E	0009056	biological_process	catabolic process
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0050490	molecular_function	1,4-lactonase activity
F	0008270	molecular_function	zinc ion binding
F	0009056	biological_process	catabolic process
F	0016787	molecular_function	hydrolase activity
F	0046872	molecular_function	metal ion binding
F	0050490	molecular_function	1,4-lactonase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 362

Chain	Residue
A	HIS24
A	HIS26
A	KCX153
A	ASP272
A	ZN363
A	HOH1197
A	HOH1198

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 363

Chain	Residue
A	HIS214
A	ZN362
A	HOH1198
A	KCX153
A	HIS186

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 364

Chain	Residue
A	LYS217
A	LYS244
A	TYR245
A	ARG275
A	TYR278
A	HOH1206

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 362

Chain	Residue
B	HIS24
B	KCX153
B	HIS186
B	HIS214
B	ZN363
B	HOH1190

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 363

Chain	Residue
B	HIS24
B	HIS26
B	KCX153
B	ASP272
B	ZN362
B	HOH1190
B	HOH1191

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 364

Chain	Residue
B	LYS244
B	TYR245
B	ARG275
B	TYR278
B	HOH931

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 362

Chain	Residue
C	HIS24
C	HIS26
C	KCX153
C	ASP272
C	HOH1192
C	HOH1193

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 363

Chain	Residue
C	KCX153
C	HIS186
C	HIS214
C	HOH1192

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 364

Chain	Residue
C	LYS244
C	TYR245
C	ARG275
C	TYR278
C	HOH1147

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 362

Chain	Residue
D	KCX153
D	HIS186
D	HIS214
D	HOH1195

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 363

Chain	Residue
D	HIS24
D	HIS26
D	KCX153
D	ASP272
D	HOH1195

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 364

Chain	Residue
D	LYS244
D	TYR245
D	ARG275
D	TYR278
D	HOH1099

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 362

Chain	Residue
E	KCX153
E	HIS186
E	HIS214
E	HOH1199

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN E 363

Chain	Residue
E	HIS24
E	HIS26
E	KCX153
E	ASP272
E	HOH1199
E	HOH1201

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 364

Chain	Residue
E	LYS217
E	LYS244
E	TYR245
E	ARG275
E	TYR278
E	HOH827
E	HOH1202

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN F 362

Chain	Residue
F	HIS24
F	HIS26
F	KCX153
F	ASP272
F	ZN363
F	HOH1196
F	HOH1200

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 363

Chain	Residue
F	KCX153
F	HIS186
F	HIS214
F	ZN362
F	HOH1196

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 F 364

Chain	Residue
F	HOH1144
F	LYS217
F	LYS244
F	TYR245
F	ARG275
F	TYR278

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:24955762, ECO:0007744\|PDB:3OVG

Chain	Residue	Details
A	HIS24
B	ASP272
C	HIS24
C	HIS26
C	HIS186
C	HIS214
C	ASP272
D	HIS24
D	HIS26
D	HIS186
D	HIS214
A	HIS26
D	ASP272
E	HIS24
E	HIS26
E	HIS186
E	HIS214
E	ASP272
F	HIS24
F	HIS26
F	HIS186
F	HIS214
A	HIS186
F	ASP272
A	HIS214
A	ASP272
B	HIS24
B	HIS26
B	HIS186
B	HIS214

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: via carbamate group => ECO:0000269\|PubMed:24955762, ECO:0007744\|PDB:3OVG

Chain	Residue	Details
A	KCX153
B	KCX153
C	KCX153
D	KCX153
E	KCX153
F	KCX153

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:24955762, ECO:0007744\|PDB:3MSR, ECO:0007744\|PDB:3OVG

Chain	Residue	Details
A	LYS244
E	ARG275
F	LYS244
F	ARG275
A	ARG275
B	LYS244
B	ARG275
C	LYS244
C	ARG275
D	LYS244
D	ARG275
E	LYS244

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:24955762, ECO:0007744\|PDB:3OVG

Chain	Residue	Details
A	KCX153
B	KCX153
C	KCX153
D	KCX153
E	KCX153
F	KCX153

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