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7AA1

Structural comparison of cellular retinoic acid binding proteins I and II in the presence and absence of natural and synthetic ligands

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0001972molecular_functionretinoic acid binding
AAA0005501molecular_functionretinoid binding
AAA0005504molecular_functionfatty acid binding
AAA0005515molecular_functionprotein binding
AAA0005634cellular_componentnucleus
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005783cellular_componentendoplasmic reticulum
AAA0005829cellular_componentcytosol
AAA0006355biological_processregulation of DNA-templated transcription
AAA0007165biological_processsignal transduction
AAA0008289molecular_functionlipid binding
AAA0008544biological_processepidermis development
AAA0015908biological_processfatty acid transport
AAA0016918molecular_functionretinal binding
AAA0019841molecular_functionretinol binding
AAA0030332molecular_functioncyclin binding
AAA0035115biological_processembryonic forelimb morphogenesis
AAA0042573biological_processretinoic acid metabolic process
AAA0048672biological_processpositive regulation of collateral sprouting
AAA0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GNWkIirSeNFEeLLKVL
ChainResidueDetails
AAAGLY6-LEU23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16979656, ECO:0007744|PDB:2FR3
ChainResidueDetails
AAAARG133

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21998312
ChainResidueDetails
AAALYS102

224572

PDB entries from 2024-09-04

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