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5X1D

Crystal Structure of T246A-N247A Human CRMP-2 Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005886cellular_componentplasma membrane
A0006139biological_processnucleobase-containing compound metabolic process
A0006208biological_processpyrimidine nucleobase catabolic process
A0006897biological_processendocytosis
A0007010biological_processcytoskeleton organization
A0007165biological_processsignal transduction
A0007399biological_processnervous system development
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0030154biological_processcell differentiation
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
ChainResidueDetails
ATYR32

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ALYS258

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942
ChainResidueDetails
ASER259

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ATYR431
ATYR499

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ASER465
ASER507

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P47942
ChainResidueDetails
ACYS504

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:10757975, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR509

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ATHR512
ATHR521

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by GSK3-beta => ECO:0007744|PubMed:21406692
ChainResidueDetails
ATHR514

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER517

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10757975, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER518

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine; by DYRK2 => ECO:0000269|PubMed:10757975, ECO:0000269|PubMed:15466863, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER522

226707

PDB entries from 2024-10-30

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