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

5EIB

Crystal structure of CPAP PN2-3 C-terminal loop-helix in complex with DARPin-tubulin

Functional Information from GO Data
ChainGOidnamespacecontents
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0007399biological_processnervous system development
D0015630cellular_componentmicrotubule cytoskeleton
D0046872molecular_functionmetal ion binding
D0046982molecular_functionprotein heterodimerization activity
D1902669biological_processpositive regulation of axon guidance
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CGLN11
CHOH654
CHOH661
CHOH687
CHOH709
CHOH733
CHOH750
CHOH777
DLYS254
CALA12
CGLN15
CASP98
CALA99
CASN101
CSER140
CGLY143

site_idAC2
Number of Residues6
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH661
CHOH666
CHOH733
CHOH777
DLYS254

site_idAC3
Number of Residues27
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DALA99
DGLY100
DASN101
DSER140
DGLY142
DGLY143
DGLY144
DTHR145
DGLY146
DVAL177
DSER178
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH615
DHOH625
DHOH626
DHOH628
DHOH640
DHOH657
DHOH683

site_idAC4
Number of Residues5
Detailsbinding site for residue MG D 502
ChainResidue
DGTP501
DHOH610
DHOH615
DHOH625
DHOH628

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
DGLY142-GLY148
CGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
DMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
DGLN11
DSER140
DGLY144
DTHR145
DGLY146
DASN206
DASN228

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
DGLU71
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
DSER40

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
ChainResidueDetails
DTHR57

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
DLYS60
CSER232

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
DSER174

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DTHR287
DTHR292

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DARG320

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
DGLU448

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DLYS60

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
CTYR451
DLYS326

site_idSWS_FT_FI12
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
CLYS326
CLYS370

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon