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1EP9

HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CONFORMATIONAL CHANGE

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_processarginine biosynthetic process
A0006591biological_processornithine metabolic process
A0006593biological_processornithine 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_processarginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0055081biological_processmonoatomic anion homeostasis
A0070781biological_processresponse to biotin
A0097272biological_processammonium homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CP A 355
ChainResidue
ASER90
ALEU304
AARG330
AHOH359
ATHR91
AARG92
ATHR93
AHIS117
AARG141
AHIS168
AGLN171
ACYS303

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:10813810
ChainResidueDetails
ACYS303

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10813810, ECO:0007744|PDB:1C9Y
ChainResidueDetails
ASER90
AARG141
AHIS168
AGLN171
ACYS303
AARG330

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:10813810, ECO:0007744|PDB:1C9Y
ChainResidueDetails
AASN199
AASP263
ASER267
AMET268

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P11725
ChainResidueDetails
ALYS70
ALYS88
ALYS144
ALYS221
ALYS231
ALYS238
ALYS292
ALYS307

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P11725
ChainResidueDetails
ALYS80
ALYS274
ALYS289

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER133

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11725
ChainResidueDetails
ALYS243

Catalytic Information from CSA
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

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PDB entries from 2024-04-24

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