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4ZR2

Crystal Structure of the Domain-Swapped Dimer K40L:Q108K:Y60W 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
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue RET A 201
ChainResidue
ALYS108

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 202
ChainResidue
ALYS107
ATRP109
BVAL62
BASP63

site_idAC3
Number of Residues2
Detailsbinding site for residue ACT A 203
ChainResidue
AGLU100
AGLU102

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT B 201
ChainResidue
BGLU89
BLYS107
BACT203
AGLU69
AHOH342

site_idAC5
Number of Residues6
Detailsbinding site for residue ACT B 202
ChainResidue
AHOH305
BASP91
BVAL92
BTRP109
BILE110
BACT203

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT B 203
ChainResidue
AHOH324
AHOH342
BTRP109
BACT201
BACT202

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18076076
ChainResidueDetails
ALEU40
ALYS108
BLEU40
BLYS108

219140

PDB entries from 2024-05-01

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