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2FS6

Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II At 1.35 Angstroms 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
B0001972molecular_functionretinoic acid binding
B0005501molecular_functionretinoid binding
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006355biological_processregulation of DNA-templated transcription
B0007165biological_processsignal transduction
B0008289molecular_functionlipid binding
B0008544biological_processepidermis development
B0015908biological_processfatty acid transport
B0016918molecular_functionretinal binding
B0019841molecular_functionretinol binding
B0030332molecular_functioncyclin binding
B0035115biological_processembryonic forelimb morphogenesis
B0042573biological_processretinoic acid metabolic process
B0048672biological_processpositive regulation of collateral sprouting
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 400
ChainResidue
BVAL41
BARG111
BLEU119
BLEU121
BTYR134
BHOH669

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 601
ChainResidue
BGLU17
BARG29
BHOH744
AACT607
AHOH766
BGLU16

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 602
ChainResidue
AVAL76
AASP77
AHOH817

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 603
ChainResidue
AARG59
AHOH821

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 604
ChainResidue
APRO39
ATHR54
ALEU121
AARG132
ATYR134
AHOH729
AHOH749

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 605
ChainResidue
AGLU73
AGLN74
ATHR75
AVAL76
AGLN97
ATRP109
AMET123
AHOH625
AHOH818

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 606
ChainResidue
BGLU73
BGLN74
BTHR75
BVAL76
BGLN97
BTRP109
BMET123
BHOH627

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 607
ChainResidue
ALYS92
AGLU112
AHOH642
BLYS30
BACT601

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AVAL21
AASP127
AVAL128
AHOH796

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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16979656, ECO:0007744|PDB:2FR3
ChainResidueDetails
AVAL133
BVAL133

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21998312
ChainResidueDetails
AGLY102
BGLY102

218853

數據於2024-04-24公開中

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