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6WNJ

The Crystal Structure of Apo Domain-Swapped Trimer Q108K:T51D:A28C:I32C 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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 201
ChainResidue
ALYS107
BTRP109
BILE110
BGLU111
CTHR1

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 202
ChainResidue
BTRP109
AASP91
AILE110
AGLU111
BTHR1

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 203
ChainResidue
AGLU89
ALYS107
BASP91

site_idAC4
Number of Residues3
Detailsbinding site for residue 144 A 204
ChainResidue
AASN59
AASP61
BLYS52

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 205
ChainResidue
AASP71
AGLU72
ATYR73

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 206
ChainResidue
ALYS101
BALA22
CGLU100
CLYS101
CGLU102

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 201
ChainResidue
AVAL62
ALYS108
BLYS40
BASP51
BTHR53

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL C 201
ChainResidue
ATHR1
CASP91
CILE110
CGLU111

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL C 202
ChainResidue
CLYS21
CPHE27
CPHE27
CARG30
CARG30
CLYS31
CHOH307

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL C 203
ChainResidue
BTYR60
BVAL62
BLYS108
CLYS40
CASP51
CTHR53

site_idAD2
Number of Residues10
Detailsbinding site for residue 144 C 204
ChainResidue
ATHR53
CTYR60
CASP61
CVAL62
CGLU72
CTYR73
CTHR74
CLYS75
CSER76
C144205

site_idAD3
Number of Residues7
Detailsbinding site for residue 144 C 205
ChainResidue
AASP51
CVAL62
CGLU72
CTRP106
CLYS108
C144204
CHOH310

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18076076
ChainResidueDetails
BLYS40
BLYS108
CLYS40
CLYS108
ALYS40
ALYS108

221051

PDB entries from 2024-06-12

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