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6MQX

Crystal Structure of All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Human Cellular Retinoic Acid Binding Protein II Irradiated with 400 nm Laser (30 seconds) and Subsequently Dark Adapted (25 minutes) at 2.0 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 Residues2
Detailsbinding site for residue GOL A 201
ChainResidue
AASN64
AGLU69

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 202
ChainResidue
AGLU62
AASN64
AGLU72
AGLU73

site_idAC3
Number of Residues10
Detailsbinding site for residue RET A 203
ChainResidue
AILE52
ATHR56
AILE63
AVAL76
ATRP109
ALYS111
AGLU121
AMET27
AILE31
ATYR39

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
AGLN132

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

218853

PDB entries from 2024-04-24

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