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3CR6

Crystal Structure of the R132K:R111L:A32E Mutant of Cellular Retinoic Acid Binding Protein Type II Complexed with C15-aldehyde (a retinal analog) at 1.22 Angstrom resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001972molecular_functionretinoic acid binding
A0005501molecular_functionretinoid binding
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0007165biological_processsignal transduction
A0008289molecular_functionlipid binding
A0008544biological_processepidermis development
A0015908biological_processfatty acid transport
A0016918molecular_functionretinal binding
A0019841molecular_functionretinol binding
A0030332molecular_functioncyclin binding
A0035115biological_processembryonic forelimb morphogenesis
A0042573biological_processretinoic acid metabolic process
A0048672biological_processpositive regulation of collateral sprouting
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LSR A 138
ChainResidue
APHE15
ALYS132
AHOH350
AALA36
APRO39
AILE52
ATHR54
ATHR61
AILE63
ALEU121
AMET123

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GNWkIirSeNFEeLLKVL
ChainResidueDetails
AGLY5-LEU22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16979656, ECO:0007744|PDB:2FR3
ChainResidueDetails
ALYS132

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21998312
ChainResidueDetails
ALYS101

217705

數據於2024-03-27公開中

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