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6HKR

Human Cellular Retinoic Acid Binding Protein II (CRABPII) with bound synthetic retinoid DC271.

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 Residues5
Detailsbinding site for residue EDO A 201
ChainResidue
AGLU74
ATRP110
AARG112
AHOH302
AHOH341

site_idAC2
Number of Residues14
Detailsbinding site for residue G9Q A 202
ChainResidue
APRO40
ATHR55
AVAL59
AVAL77
AASP78
ALEU122
AARG133
ATYR135
AHOH321
AHOH341
AARG12
ALEU29
AALA33
AALA37

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 203
ChainResidue
AARG12
ALEU23
AGLY24
AASP78
AHOH395
AHOH418

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 204
ChainResidue
ASER13
AGLU14
AASN15
APHE16
AGLU17
AGLU18
AHOH319
AHOH367
AHOH382
AHOH398

site_idAC5
Number of Residues10
Detailsbinding site for residue PG4 A 205
ChainResidue
AILE32
ATHR58
AVAL59
ATHR123
AVAL130
AHOH311
AHOH342
AHOH363
AHOH364
AHOH403

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16979656, ECO:0007744|PDB:2FR3
ChainResidueDetails
AARG133

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21998312
ChainResidueDetails
ALYS102

223532

PDB entries from 2024-08-07

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