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1FVO

CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMYLASE COMPLEXED WITH CARBAMOYL PHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0001889biological_processliver development
A0004585molecular_functionornithine carbamoyltransferase activity
A0005543molecular_functionphospholipid binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006520biological_processamino acid metabolic process
A0006526biological_processL-arginine biosynthetic process
A0006591biological_processornithine metabolic process
A0006593biological_processL-ornithine catabolic process
A0007494biological_processmidgut development
A0008652biological_processamino acid biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0010043biological_processresponse to zinc ion
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0019240biological_processcitrulline biosynthetic process
A0031667biological_processresponse to nutrient levels
A0032868biological_processresponse to insulin
A0042301molecular_functionphosphate ion binding
A0042450biological_processL-arginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0055081biological_processmonoatomic anion homeostasis
A0070781biological_processresponse to biotin
A0097272biological_processammonium homeostasis
B0000050biological_processurea cycle
B0001889biological_processliver development
B0004585molecular_functionornithine carbamoyltransferase activity
B0005543molecular_functionphospholipid binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0006520biological_processamino acid metabolic process
B0006526biological_processL-arginine biosynthetic process
B0006591biological_processornithine metabolic process
B0006593biological_processL-ornithine catabolic process
B0007494biological_processmidgut development
B0008652biological_processamino acid biosynthetic process
B0009410biological_processresponse to xenobiotic stimulus
B0010043biological_processresponse to zinc ion
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0019240biological_processcitrulline biosynthetic process
B0031667biological_processresponse to nutrient levels
B0032868biological_processresponse to insulin
B0042301molecular_functionphosphate ion binding
B0042450biological_processL-arginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
B0055081biological_processmonoatomic anion homeostasis
B0070781biological_processresponse to biotin
B0097272biological_processammonium homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CP A 355
ChainResidue
ASER90
ALEU304
AARG330
ATHR91
AARG92
ATHR93
AHIS117
AARG141
AHIS168
AGLN171
ACYS303

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CP B 355
ChainResidue
BSER90
BTHR91
BARG92
BTHR93
BHIS117
BARG141
BHIS168
BGLN171
BCYS303
BLEU304
BARG330

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FeKrSTRT
ChainResidueDetails
APHE86-THR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10813810","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10813810","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C9Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10813810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1C9Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1akm
ChainResidueDetails
AARG141
AASP263
AARG330
AGLN171
ACYS303
AHIS168

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1akm
ChainResidueDetails
BARG141
BASP263
BARG330
BGLN171
BCYS303
BHIS168

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1akm
ChainResidueDetails
AARG92
AARG141
ATHR93
AHIS168

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1akm
ChainResidueDetails
BARG92
BARG141
BTHR93
BHIS168

site_idMCSA1
Number of Residues6
DetailsM-CSA 12
ChainResidueDetails
AARG141electrostatic stabiliser, hydrogen bond donor
AHIS168electrostatic stabiliser, hydrogen bond donor
AGLN171activator, hydrogen bond acceptor
AASP263activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS303hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG330electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 12
ChainResidueDetails
BARG141electrostatic stabiliser, hydrogen bond donor
BHIS168electrostatic stabiliser, hydrogen bond donor
BGLN171activator, hydrogen bond acceptor
BASP263activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS303hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BARG330electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-07-09

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