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5EIB

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

Functional Information from GO Data
ChainGOidnamespacecontents
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003725molecular_functiondouble-stranded RNA binding
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0005881cellular_componentcytoplasmic microtubule
C0005929cellular_componentcilium
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0030182biological_processneuron differentiation
C0031625molecular_functionubiquitin protein ligase binding
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0001764biological_processneuron migration
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
CGLY142-GLY148
DGLY142-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 Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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