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1PMP

CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOL

Functional Information from GO Data
ChainGOidnamespacecontents
A0005504molecular_functionfatty acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0015485molecular_functioncholesterol binding
A0015908biological_processfatty acid transport
A0043209cellular_componentmyelin sheath
A0061024biological_processmembrane organization
B0005504molecular_functionfatty acid binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008289molecular_functionlipid binding
B0015485molecular_functioncholesterol binding
B0015908biological_processfatty acid transport
B0043209cellular_componentmyelin sheath
B0061024biological_processmembrane organization
C0005504molecular_functionfatty acid binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008289molecular_functionlipid binding
C0015485molecular_functioncholesterol binding
C0015908biological_processfatty acid transport
C0043209cellular_componentmyelin sheath
C0061024biological_processmembrane organization
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLA A 200
ChainResidue
AMET20
ATHR29
AARG106
AARG126
ATYR128

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLA B 200
ChainResidue
BARG106
BARG126
BTYR128
BMET20
BTHR29
BGLY33
BTHR53

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLA C 200
ChainResidue
CPHE16
CTHR29
CTHR53
CARG106
CARG126
CTYR128

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P02689","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6156092","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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