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4CNS

Crystal structure of truncated human CRMP-4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0005737cellular_componentcytoplasm
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG C 1489
ChainResidue
CILE240
CHOH2122
DGLU230
CSER244
CLEU263
CGLN266
CALA267
CLYS270
CASN272
CHOH2071
CHOH2088

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1490
ChainResidue
AGLU230
AALA233
ASER259
BLYS270

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1491
ChainResidue
APHE237
ALYS270
AHOH2099
AHOH2106

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1492
ChainResidue
AALA300
APHE336
ALYS341
AGLY354
AASN356
AALA429
ATYR431

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 1490
ChainResidue
DTYR170
DARG227
DHOH2061

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1493
ChainResidue
ATYR170
AARG227
AHOH2067

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1489
ChainResidue
BTYR170
BARG227

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 1490
ChainResidue
CTYR170
CILE205
CARG227
CHOH2046

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 1490
ChainResidue
BASP128
BGLY464
BGLY466
BHOH2037

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 1491
ChainResidue
DASP128
DGLY464
DGLY466

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 1491
ChainResidue
CASP128
CGLY464
CGLY466

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1494
ChainResidue
AASP128
AGLY464
AGLY466

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1495
ChainResidue
ALYS254
AILE279
ATHR303
AHOH2103
AHOH2119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER259
BSER259
CSER259
DSER259

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62188
ChainResidueDetails
ATYR431
BTYR431
CTYR431
DTYR431

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PDB entries from 2024-10-09

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