Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5GV2

Crystal structure of Arginine-bound CASTOR1 from Homo sapiens

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0034198biological_processcellular response to amino acid starvation
A0034618molecular_functionarginine binding
A0042802molecular_functionidentical protein binding
A0061700cellular_componentGATOR2 complex
A0140299molecular_functionsmall molecule sensor activity
A0140311molecular_functionprotein sequestering activity
A1903577biological_processcellular response to L-arginine
A1904262biological_processnegative regulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0034198biological_processcellular response to amino acid starvation
C0034618molecular_functionarginine binding
C0042802molecular_functionidentical protein binding
C0061700cellular_componentGATOR2 complex
C0140299molecular_functionsmall molecule sensor activity
C0140311molecular_functionprotein sequestering activity
C1903577biological_processcellular response to L-arginine
C1904262biological_processnegative regulation of TORC1 signaling
C1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG C 501
ChainResidue
AHIS108
AHIS135
CHIS108
CHIS135

site_idAC2
Number of Residues16
Detailsbinding site for residue ARG A 401
ChainResidue
ACYS278
AGLY279
AILE280
AVAL281
ASER299
ATHR300
APHE301
APHE303
AASP304
AHOH538
AHOH547
ASER111
AVAL112
ALEU273
AGLY274
AGLU277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27487210, ECO:0007744|PDB:5I2C
ChainResidueDetails
CSER111
CGLY274
CILE280
CTHR300
ASER111
AGLY274
AILE280
ATHR300

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:33594058
ChainResidueDetails
CSER14
ASER14

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon