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5I2C

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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0034198biological_processcellular response to amino acid starvation
B0034618molecular_functionarginine binding
B0042802molecular_functionidentical protein binding
B0061700cellular_componentGATOR2 complex
B0140299molecular_functionsmall molecule sensor activity
B0140311molecular_functionprotein sequestering activity
B1903577biological_processcellular response to L-arginine
B1904262biological_processnegative regulation of TORC1 signaling
B1904263biological_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
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0034198biological_processcellular response to amino acid starvation
D0034618molecular_functionarginine binding
D0042802molecular_functionidentical protein binding
D0061700cellular_componentGATOR2 complex
D0140299molecular_functionsmall molecule sensor activity
D0140311molecular_functionprotein sequestering activity
D1903577biological_processcellular response to L-arginine
D1904262biological_processnegative regulation of TORC1 signaling
D1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ARG A 401
ChainResidue
ASER111
ATHR300
APHE301
APHE303
AASP304
AHOH577
AHOH594
AHOH623
AVAL112
ALEU273
AGLY274
AGLU277
ACYS278
AGLY279
AILE280
AVAL281

site_idAC2
Number of Residues9
Detailsbinding site for residue ACT A 402
ChainResidue
ALEU115
ASER116
ATHR117
AALA229
ASER231
ASER238
AVAL240
AILE298
AHOH513

site_idAC3
Number of Residues17
Detailsbinding site for residue ARG B 401
ChainResidue
BSER111
BVAL112
BLEU273
BGLY274
BGLU277
BCYS278
BGLY279
BILE280
BVAL281
BSER299
BTHR300
BPHE301
BPHE303
BASP304
BHOH549
BHOH552
BHOH577

site_idAC4
Number of Residues7
Detailsbinding site for residue ACT B 402
ChainResidue
BLEU115
BSER116
BTHR117
BALA229
BSER231
BSER238
BILE298

site_idAC5
Number of Residues17
Detailsbinding site for residue ARG C 401
ChainResidue
CSER111
CVAL112
CLEU273
CGLY274
CGLU277
CCYS278
CGLY279
CILE280
CVAL281
CSER299
CTHR300
CPHE301
CPHE303
CASP304
CHOH566
CHOH572
CHOH592

site_idAC6
Number of Residues7
Detailsbinding site for residue ACT C 402
ChainResidue
CSER116
CTHR117
CSER231
CSER238
CVAL240
CILE298
CHOH506

site_idAC7
Number of Residues16
Detailsbinding site for residue ARG D 401
ChainResidue
DSER111
DVAL112
DLEU273
DGLY274
DGLU277
DCYS278
DGLY279
DILE280
DVAL281
DTHR300
DPHE301
DPHE303
DASP304
DHOH529
DHOH540
DHOH581

site_idAC8
Number of Residues6
Detailsbinding site for residue ACT D 402
ChainResidue
DLEU115
DSER116
DSER231
DSER238
DILE298
DHOH514

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27487210, ECO:0007744|PDB:5I2C
ChainResidueDetails
ASER111
CGLY274
CILE280
CTHR300
DSER111
DGLY274
DILE280
DTHR300
AGLY274
AILE280
ATHR300
BSER111
BGLY274
BILE280
BTHR300
CSER111

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:33594058
ChainResidueDetails
ASER14
BSER14
CSER14
DSER14

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PDB entries from 2024-04-24

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