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4A1Y

Human myelin P2 protein, K65Q mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0015485molecular_functioncholesterol binding
A0015908biological_processfatty acid transport
A0043209cellular_componentmyelin sheath
A0061024biological_processmembrane organization
A0070062cellular_componentextracellular exosome
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PLM A 1132
ChainResidue
ASER55
AARG106
AARG126
ATYR128
AHOH1157
AHOH1221

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1133
ChainResidue
ALYS37
ASER55
ATHR56

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PLM B 1132
ChainResidue
BMET20
BTHR29
BASP76
BARG106
BARG126
BTYR128
BHOH1336
BHOH1351

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PLM C 1132
ChainResidue
CMET20
CGLY33
CARG106
CARG126
CTYR128
CHOH1369
CHOH1370

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1133
ChainResidue
CLYS37
CSER55
CTHR56

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 1132
ChainResidue
DLYS37
DSER55
DTHR56

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PLM D 1133
ChainResidue
DASP76
DARG106
DARG126
DTYR128
DHOH1354
DHOH1355

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKAL
ChainResidueDetails
AGLY6-LEU23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20421974, ECO:0007744|PDB:2WUT
ChainResidueDetails
AARG106
AARG126
BARG106
BARG126
CARG106
CARG126
DARG106
DARG126

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6183401
ChainResidueDetails
ASER1
BSER1
CSER1
DSER1

224931

PDB entries from 2024-09-11

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