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

3FM8

Crystal structure of full length centaurin alpha-1 bound with the FHA domain of KIF13B (CAPRI target)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005911cellular_componentcell-cell junction
B0005911cellular_componentcell-cell junction
C0005096molecular_functionGTPase activator activity
C0005515molecular_functionprotein binding
C0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0007166biological_processcell surface receptor signaling pathway
C0043087biological_processregulation of GTPase activity
C0043231cellular_componentintracellular membrane-bounded organelle
C0043533molecular_functioninositol 1,3,4,5 tetrakisphosphate binding
C0043547biological_processpositive regulation of GTPase activity
C0046872molecular_functionmetal ion binding
C1902936molecular_functionphosphatidylinositol bisphosphate binding
D0005096molecular_functionGTPase activator activity
D0005515molecular_functionprotein binding
D0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0007166biological_processcell surface receptor signaling pathway
D0043087biological_processregulation of GTPase activity
D0043231cellular_componentintracellular membrane-bounded organelle
D0043533molecular_functioninositol 1,3,4,5 tetrakisphosphate binding
D0043547biological_processpositive regulation of GTPase activity
D0046872molecular_functionmetal ion binding
D1902936molecular_functionphosphatidylinositol bisphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 401
ChainResidue
CCYS21
CCYS24
CCYS41
CCYS44

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 375
ChainResidue
CARG156
CLYS3
CGLU4
CARG5
CARG6
CTRP65

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 401
ChainResidue
DCYS21
DCYS24
DCYS41
DCYS44

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 375
ChainResidue
DHIS193
DGLU213
DASP214
DGLY215
DHOH422
DHOH434

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 376
ChainResidue
DLYS261
DARG273
DTYR284
DARG294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsZN_FING: C4-type => ECO:0000255|PROSITE-ProRule:PRU00288
ChainResidueDetails
CCYS21-CYS44
DCYS21-CYS44

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:12893243
ChainResidueDetails
CSER87
DSER87

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS272
DLYS272

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12893243
ChainResidueDetails
CTHR276
DTHR276

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon