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4QYP

The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinal

Functional Information from GO Data
ChainGOidnamespacecontents
A0005501molecular_functionretinoid binding
A0005504molecular_functionfatty acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006776biological_processvitamin A metabolic process
A0008289molecular_functionlipid binding
A0008544biological_processepidermis development
A0015908biological_processfatty acid transport
A0016918molecular_functionretinal binding
A0019841molecular_functionretinol binding
B0005501molecular_functionretinoid binding
B0005504molecular_functionfatty acid binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006776biological_processvitamin A metabolic process
B0008289molecular_functionlipid binding
B0008544biological_processepidermis development
B0015908biological_processfatty acid transport
B0016918molecular_functionretinal binding
B0019841molecular_functionretinol binding
C0005501molecular_functionretinoid binding
C0005504molecular_functionfatty acid binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006776biological_processvitamin A metabolic process
C0008289molecular_functionlipid binding
C0008544biological_processepidermis development
C0015908biological_processfatty acid transport
C0016918molecular_functionretinal binding
C0019841molecular_functionretinol binding
D0005501molecular_functionretinoid binding
D0005504molecular_functionfatty acid binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006776biological_processvitamin A metabolic process
D0008289molecular_functionlipid binding
D0008544biological_processepidermis development
D0015908biological_processfatty acid transport
D0016918molecular_functionretinal binding
D0019841molecular_functionretinol binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RET A 201
ChainResidue
APHE16
ATHR51
APHE57
ASER76
ALEU77
ATRP106
ALEU119
AHOH358

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RET B 201
ChainResidue
BLYS40
BTHR51
BTHR53
BLEU77
BTRP106
BGLN108
BHOH310
BPHE16

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 202
ChainResidue
BASP24
BASP26
BASP78
BHOH357

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 203
ChainResidue
ATHR1
AASP91
BASP63

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 204
ChainResidue
BVAL34
BHOH375
CHOH308
CHOH324
CHOH337

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RET C 201
ChainResidue
CILE25
CLYS40
CTHR51
CVAL62
CPHE64
CLEU77
CTRP106
CACT202
CHOH304

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 202
ChainResidue
CTYR60
CGLU72
CGLN97
CRET201
CHOH386

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18076076
ChainResidueDetails
ALYS40
AGLN108
BLYS40
BGLN108
CLYS40
CGLN108
DLYS40
DGLN108

218853

數據於2024-04-24公開中

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