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

4B90

Crystal structure of WT human CRMP-5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006208biological_processpyrimidine nucleobase catabolic process
A0007165biological_processsignal transduction
A0007399biological_processnervous system development
A0007411biological_processaxon guidance
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
A0030182biological_processneuron differentiation
A0030425cellular_componentdendrite
A0032991cellular_componentprotein-containing complex
A0043025cellular_componentneuronal cell body
A0050774biological_processnegative regulation of dendrite morphogenesis
B0004157molecular_functiondihydropyrimidinase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006208biological_processpyrimidine nucleobase catabolic process
B0007165biological_processsignal transduction
B0007399biological_processnervous system development
B0007411biological_processaxon guidance
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0030182biological_processneuron differentiation
B0030425cellular_componentdendrite
B0032991cellular_componentprotein-containing complex
B0043025cellular_componentneuronal cell body
B0050774biological_processnegative regulation of dendrite morphogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1492
ChainResidue
AGLN36
AGLN37
AVAL38
APRO396

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1493
ChainResidue
BASP20
BASN371
BARG372
BALA375
BHOH2060

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9EQF6
ChainResidueDetails
ATHR509
ATHR514
BTHR509
BTHR514

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9EQF6
ChainResidueDetails
ASER532
ASER538
BSER532
BSER538

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q9EQF6
ChainResidueDetails
AARG559
BARG559

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon