1DUV

CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)

Functional Information from GO Data

Chain	GOid	namespace	contents
G	0003824	molecular_function	catalytic activity
G	0004585	molecular_function	ornithine carbamoyltransferase activity
G	0005737	cellular_component	cytoplasm
G	0006520	biological_process	amino acid metabolic process
G	0006526	biological_process	L-arginine biosynthetic process
G	0006591	biological_process	ornithine metabolic process
G	0008652	biological_process	amino acid biosynthetic process
G	0016597	molecular_function	amino acid binding
G	0016740	molecular_function	transferase activity
G	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
G	0019240	biological_process	citrulline biosynthetic process
G	0042450	biological_process	L-arginine biosynthetic process via ornithine
G	0046872	molecular_function	metal ion binding
H	0003824	molecular_function	catalytic activity
H	0004585	molecular_function	ornithine carbamoyltransferase activity
H	0005737	cellular_component	cytoplasm
H	0006520	biological_process	amino acid metabolic process
H	0006526	biological_process	L-arginine biosynthetic process
H	0006591	biological_process	ornithine metabolic process
H	0008652	biological_process	amino acid biosynthetic process
H	0016597	molecular_function	amino acid binding
H	0016740	molecular_function	transferase activity
H	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
H	0019240	biological_process	citrulline biosynthetic process
H	0042450	biological_process	L-arginine biosynthetic process via ornithine
H	0046872	molecular_function	metal ion binding
I	0003824	molecular_function	catalytic activity
I	0004585	molecular_function	ornithine carbamoyltransferase activity
I	0005737	cellular_component	cytoplasm
I	0006520	biological_process	amino acid metabolic process
I	0006526	biological_process	L-arginine biosynthetic process
I	0006591	biological_process	ornithine metabolic process
I	0008652	biological_process	amino acid biosynthetic process
I	0016597	molecular_function	amino acid binding
I	0016740	molecular_function	transferase activity
I	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
I	0019240	biological_process	citrulline biosynthetic process
I	0042450	biological_process	L-arginine biosynthetic process via ornithine
I	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PSQ G 401

Chain	Residue
G	SER55
G	ASN167
G	ASP231
G	SER235
G	MET236
G	CYS273
G	LEU274
G	ARG319
G	HOH606
I	GLN82
I	HOH598
G	THR56
G	ARG57
G	THR58
G	ARG106
G	LEU128
G	HIS133
G	GLN136
G	ASN166

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PSQ H 402

Chain	Residue
G	GLN82
H	SER55
H	THR56
H	ARG57
H	THR58
H	ARG106
H	HIS133
H	GLN136
H	ASN166
H	ASN167
H	ASP231
H	SER235
H	MET236
H	CYS273
H	LEU274
H	ARG319
H	HOH602
H	HOH611

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PSQ I 403

Chain	Residue
H	GLN82
I	SER55
I	THR56
I	ARG57
I	THR58
I	ARG106
I	HIS133
I	GLN136
I	ASN166
I	ASN167
I	ASP231
I	SER235
I	MET236
I	CYS273
I	LEU274
I	ARG319
I	HOH604
I	HOH773

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD G 404

Chain	Residue
G	LEU25
G	ALA329
G	LYS333
G	HOH538
G	HOH1149
H	LYS151

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
G	PHE51-THR58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10747936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9275160","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DUV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OTC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2405164","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10747936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DUV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
G	GLN136
G	CYS273
G	ASP231
G	ARG106
G	HIS133
G	ARG319

---

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
H	GLN136
H	CYS273
H	ASP231
H	ARG106
H	HIS133
H	ARG319

---

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
I	GLN136
I	CYS273
I	ASP231
I	ARG106
I	HIS133
I	ARG319

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
G	THR58
G	ARG106
G	HIS133
G	ARG57

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
H	THR58
H	ARG106
H	HIS133
H	ARG57

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1akm

Chain	Residue	Details
I	THR58
I	ARG106
I	HIS133
I	ARG57

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