Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H31

Crystal structure of anabolic ornithine carbamoyltransferase from Vibrio vulnificus in complex with carbamoyl phosphate and L-norvaline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004585	molecular_function	ornithine carbamoyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0006526	biological_process	L-arginine biosynthetic process
A	0006591	biological_process	ornithine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
A	0019240	biological_process	citrulline biosynthetic process
A	0042450	biological_process	L-arginine biosynthetic process via ornithine
B	0004585	molecular_function	ornithine carbamoyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
B	0006526	biological_process	L-arginine biosynthetic process
B	0006591	biological_process	ornithine metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
B	0019240	biological_process	citrulline biosynthetic process
B	0042450	biological_process	L-arginine biosynthetic process via ornithine
C	0004585	molecular_function	ornithine carbamoyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0006520	biological_process	amino acid metabolic process
C	0006526	biological_process	L-arginine biosynthetic process
C	0006591	biological_process	ornithine metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016597	molecular_function	amino acid binding
C	0016740	molecular_function	transferase activity
C	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
C	0019240	biological_process	citrulline biosynthetic process
C	0042450	biological_process	L-arginine biosynthetic process via ornithine

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NVA A 401

Chain	Residue
A	ASN168
A	ASN169
A	ASP233
A	SER237
A	MET238
A	LEU276
A	CP402
A	HOH514
B	HOH503

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CP A 402

Chain	Residue
A	SER57
A	THR58
A	ARG59
A	THR60
A	ARG108
A	HIS135
A	GLN138
A	CYS275
A	LEU276
A	ARG320
A	NVA401
B	GLN84

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PE5 A 403

Chain	Residue
A	GLU307
A	HOH676
B	ALA120
B	PHE121
B	ARG186
B	THR215
B	GLU222

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 404

Chain	Residue
A	GLU218
A	ASN219
A	VAL220
A	HOH573
A	HOH590

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 405

Chain	Residue
A	ASP132
A	MET238
A	GLY239
A	GLU240

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 406

Chain	Residue
A	LYS263
A	ASN267
A	PRO268
A	HIS310

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 407

Chain	Residue
A	LEU13
A	PHE134
A	SER173
A	HOH505

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 408

Chain	Residue
A	THR215
A	GLU222

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 409

Chain	Residue
A	GLU116
A	ASN260
A	GLN264
A	HOH575

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 410

Chain	Residue
A	LYS253
A	GLN256
A	ASN258
A	HOH542

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 411

Chain	Residue
A	ASN258
A	MET259
A	THR302

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 412

Chain	Residue
A	ARG96
A	GLN225
A	HOH617
C	PHE306
C	GLU307
C	SER311
C	PHE314
C	HOH612

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG A 413

Chain	Residue
A	ASP30

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NVA B 401

Chain	Residue
B	ASN168
B	ASN169
B	ASP233
B	SER237
B	MET238
B	LEU276
B	CP402
B	HOH515
C	HOH531

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CP B 402

Chain	Residue
B	SER57
B	THR58
B	ARG59
B	THR60
B	ARG108
B	HIS135
B	GLN138
B	CYS275
B	LEU276
B	ARG320
B	NVA401
C	GLN84

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 403

Chain	Residue
B	ALA205
B	GLN209
B	LYS253
B	PHE294
B	HOH637

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 404

Chain	Residue
B	LEU13
B	PHE134
B	SER173

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 405

Chain	Residue
B	LEU262
B	ASN267
B	HIS310

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 406

Chain	Residue
B	ASN258
B	MET259
B	THR302
B	GLU304

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 407

Chain	Residue
A	GLU283
A	THR285
B	GLY86

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 408

Chain	Residue
B	ALA156
B	ASP157
B	ILE158
B	GLY182
B	GLY211

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 409

Chain	Residue
B	ALA29
B	LYS32
B	GLU148

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PE5 B 410

Chain	Residue
B	ASP132
B	ARG167
B	MET238
B	GLY239

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 411

Chain	Residue
B	SER17
B	THR18
B	LYS180
B	LYS253

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NVA C 401

Chain	Residue
A	HOH540
C	ASN168
C	ASN169
C	ASP233
C	SER237
C	MET238
C	LEU276
C	CP403
C	HOH511

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 402

Chain	Residue
C	LEU13
C	SER173

site_id	CC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CP C 403

Chain	Residue
A	GLN84
C	SER57
C	THR58
C	ARG59
C	THR60
C	ARG108
C	HIS135
C	GLN138
C	CYS275
C	LEU276
C	ARG320
C	NVA401

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PE5 C 404

Chain	Residue
C	ASP132
C	ARG167
C	MET238
C	HOH526

site_id	DC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 405

Chain	Residue
C	THR215
C	GLU222

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG C 406

Chain	Residue
C	LEU262
C	ASN267
C	HIS310

site_id	DC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG C 407

Chain	Residue
A	GLN264

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 408

Chain	Residue
C	ASN258
C	MET259
C	THR302
C	GLU304

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG C 409

Chain	Residue
C	SER237
C	MET238
C	GLY239
C	GLU240
C	HOH514
C	HOH546
C	HOH591

Functional Information from PROSITE/UniProt

site_id	PS00097
Number of Residues	8
Details	CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FeKaSTRT

Chain	Residue	Details
A	PHE53-THR60

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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