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4QZT

Crystal Structure of wild type Human Cellular Retinol Binding Protein II (hCRBPII) bound to retinol at 7 KeV beam energy

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 Residues10
DetailsBINDING SITE FOR RESIDUE RTL A 201
ChainResidue
APHE16
AACT202
ALYS40
ATHR51
ASER76
ALEU77
ATRP106
AGLN108
ALEU117
ALEU119

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 202
ChainResidue
ATYR60
AGLU72
ATHR74
ALEU77
AGLN97
ARTL201
AHOH334

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE RTL C 201
ChainResidue
CPHE16
CALA33
CGLN38
CLYS40
CSER76
CLEU77
CTRP106
CGLN108
CLEU119
CACT202
CHOH345

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 202
ChainResidue
CGLU72
CGLN97
CTRP106
CRTL201
CHOH314

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 201
ChainResidue
BTYR60
BGLU72
BLEU77
BGLN97
BHOH302
BHOH355

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
CLYS40
CGLN108
BLYS40
BGLN108
DLYS40
DGLN108

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PDB entries from 2024-11-06

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