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6VID

The Crystal Structure of Aps Domain-Swapped Trimer Q108K:K40D:T53A:R58L:Q38F:Q4F Variant of HCRBPII

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
E0005501molecular_functionretinoid binding
E0005504molecular_functionfatty acid binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006776biological_processvitamin A metabolic process
E0008289molecular_functionlipid binding
E0008544biological_processepidermis development
E0015908biological_processfatty acid transport
E0016918molecular_functionretinal binding
E0019841molecular_functionretinol binding
F0005501molecular_functionretinoid binding
F0005504molecular_functionfatty acid binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006776biological_processvitamin A metabolic process
F0008289molecular_functionlipid binding
F0008544biological_processepidermis development
F0015908biological_processfatty acid transport
F0016918molecular_functionretinal binding
F0019841molecular_functionretinol binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue ACT A 201
ChainResidue
AASP26
DLYS31

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 202
ChainResidue
AILE25
BTHR1
BASP3
BGOL202

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 203
ChainResidue
ATRP106
ATYR60
AGLU72
ALEU77

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 204
ChainResidue
ASER76
BASP40

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 205
ChainResidue
APHE38
AASP40
DSER76
DGLN128

site_idAC6
Number of Residues1
Detailsbinding site for residue ACT B 201
ChainResidue
BTRP106

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 202
ChainResidue
AASP26
AACT202
BARG2
BGLY46
DPHE27

site_idAC8
Number of Residues2
Detailsbinding site for residue GOL D 201
ChainResidue
DMET10
DASN59

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 Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18076076
ChainResidueDetails
AASP40
ELYS108
FASP40
FLYS108
ALYS108
BASP40
BLYS108
CASP40
CLYS108
DASP40
DLYS108
EASP40

222926

PDB entries from 2024-07-24

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