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6MKV

Crystal structure of Retinal-bound holo Q108K:K40L:T51W domain-swapped dimer of human cellular retinol binding protein 2

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 Residues4
Detailsbinding site for residue ACT B 202
ChainResidue
BASN5
BGLY6
BILE42
BASP43

site_idAC2
Number of Residues5
Detailsbinding site for residue ACT B 203
ChainResidue
BASP91
BVAL92
BTRP109
BILE110
DTHR1

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL B 204
ChainResidue
BARG127
DSER12
DGLU14

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT C 202
ChainResidue
BARG35
BPHE57
BARG58
CGLU118
CARG127

site_idAC5
Number of Residues4
Detailsbinding site for residue ACT D 202
ChainResidue
DTYR60
DASP61
DVAL62
DTYR73

site_idAC6
Number of Residues3
Detailsbinding site for residue ACT D 203
ChainResidue
BTRP88
DARG2
DASP47

site_idAC7
Number of Residues2
Detailsbinding site for residue ACT D 204
ChainResidue
DMET10
DGLU11

site_idAC8
Number of Residues5
Detailsbinding site for residue ACT D 205
ChainResidue
DTYR60
DGLU72
DLEU77
DGLN97
DTRP106

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL D 206
ChainResidue
DARG2
DGLN44
DASP45
DGLY46

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
ALEU40
ALYS108
BLEU40
BLYS108
CLEU40
CLYS108
DLEU40
DLYS108

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PDB entries from 2024-06-19

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