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6XVY

Human myelin protein P2 mutant R88Q

Functional Information from GO Data
ChainGOidnamespacecontents
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008289molecular_functionlipid binding
B0015485molecular_functioncholesterol binding
B0015908biological_processfatty acid transport
B0043209cellular_componentmyelin sheath
B0061024biological_processmembrane organization
B0070062cellular_componentextracellular exosome
C0005504molecular_functionfatty acid binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008289molecular_functionlipid binding
C0015485molecular_functioncholesterol binding
C0015908biological_processfatty acid transport
C0043209cellular_componentmyelin sheath
C0061024biological_processmembrane organization
C0070062cellular_componentextracellular exosome
D0005504molecular_functionfatty acid binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008289molecular_functionlipid binding
D0015485molecular_functioncholesterol binding
D0015908biological_processfatty acid transport
D0043209cellular_componentmyelin sheath
D0061024biological_processmembrane organization
D0070062cellular_componentextracellular exosome
E0005504molecular_functionfatty acid binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0008289molecular_functionlipid binding
E0015485molecular_functioncholesterol binding
E0015908biological_processfatty acid transport
E0043209cellular_componentmyelin sheath
E0061024biological_processmembrane organization
E0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PLM B 201
ChainResidue
BGLY33
BPRO38
BALA75
BASP76
BARG106
BARG126
BTYR128
BHOH324
BHOH353

site_idAC2
Number of Residues2
Detailsbinding site for residue CL B 202
ChainResidue
BLYS37
BTHR56

site_idAC3
Number of Residues7
Detailsbinding site for residue PLM C 201
ChainResidue
CPHE16
CASP76
CARG106
CARG126
CTYR128
CHOH332
CHOH369

site_idAC4
Number of Residues4
Detailsbinding site for residue CL C 202
ChainResidue
CLYS37
CSER55
CTHR56
CHOH463

site_idAC5
Number of Residues13
Detailsbinding site for residue CIT C 203
ChainResidue
CGLY26
CLEU27
CALA28
CTHR29
CHOH317
CHOH358
CHOH367
CHOH376
EALA28
ETHR29
ELYS100
EHOH355
EHOH381

site_idAC6
Number of Residues8
Detailsbinding site for residue PLM D 201
ChainResidue
DMET20
DTHR29
DGLY33
DARG106
DARG126
DTYR128
DHOH317
DHOH341

site_idAC7
Number of Residues3
Detailsbinding site for residue CL D 202
ChainResidue
DLYS37
DSER55
DTHR56

site_idAC8
Number of Residues4
Detailsbinding site for residue CIT D 203
ChainResidue
DGLU69
DHOH347
EGLN88
EHOH402

site_idAC9
Number of Residues6
Detailsbinding site for residue PLM E 201
ChainResidue
EASP76
EARG106
ECYS117
EARG126
ETYR128
EHOH308

site_idAD1
Number of Residues4
Detailsbinding site for residue CL E 202
ChainResidue
ELYS37
ESER55
ETHR56
EHOH318

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKAL
ChainResidueDetails
BGLY6-LEU23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20421974, ECO:0007744|PDB:2WUT
ChainResidueDetails
BARG106
BARG126
CARG106
CARG126
DARG106
DARG126
EARG106
EARG126

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6183401
ChainResidueDetails
BSER1
CSER1
DSER1
ESER1

223166

PDB entries from 2024-07-31

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