Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6E7M

Crystal structure of the holo retinal-bound domain-swapped dimer Q108K:T51D:A28C mutant of human Cellular Retinol Binding Protein II

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 Residues6
Detailsbinding site for residue ACT A 201
ChainResidue
AHIS81
AGLU100
DTRP109
DTYR116
DLEU117
DGLU118

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 202
ChainResidue
DARG80
AARG35
ATHR37
DASN79

site_idAC3
Number of Residues6
Detailsbinding site for residue ACT A 203
ChainResidue
ALYS40
AASP51
CTRP106
CLYS108
CLEU117
CLEU119

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 204
ChainResidue
AGLY6
ATHR7
ALYS21
AILE25
AARG30
AVAL41
AASP43
AHOH301

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 205
ChainResidue
AGLN38
ATHR53
AHOH305
CTYR60
CGLN128

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 206
ChainResidue
AASN48
APHE49
ALYS50
BARG127
CASP63
CPHE64
CTHR65

site_idAC7
Number of Residues1
Detailsbinding site for residue ACT B 201
ChainResidue
BVAL92

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL B 202
ChainResidue
AVAL125
AARG127
BHIS81
BGLU100
CGLU14

site_idAC9
Number of Residues3
Detailsbinding site for residue ACT C 201
ChainResidue
ALYS114
ATYR116
CGLU11

site_idAD1
Number of Residues3
Detailsbinding site for residue ACT C 202
ChainResidue
AASP47
CARG30
CTRP88

site_idAD2
Number of Residues5
Detailsbinding site for residue ACT C 203
ChainResidue
ALEU23
AASP24
CASP78
CARG80
CLYS133

site_idAD3
Number of Residues1
Detailsbinding site for residue ACT C 204
ChainResidue
CPHE16

site_idAD4
Number of Residues5
Detailsbinding site for residue ACT C 205
ChainResidue
ATYR19
CTYR60
CGLN97
CARG104
CLEU119

site_idAD5
Number of Residues6
Detailsbinding site for residue GOL C 206
ChainResidue
CASN5
CGLY6
CVAL41
CILE42
CASN103
CGLY122

site_idAD6
Number of Residues6
Detailsbinding site for residue ACT D 201
ChainResidue
DTYR60
DVAL62
DGLU72
DCYS95
DGLN97
DTRP106

site_idAD7
Number of Residues8
Detailsbinding site for residue GOL D 202
ChainResidue
DVAL94
DCYS95
DVAL96
DASN103
DGLY105
DTRP106
DLYS107
DTHR120

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
ALYS108
BLYS40
BLYS108
CLYS40
CLYS108
DLYS40
DLYS108

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon