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4EFG

Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.58 Angstrom Resolution

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 Residues10
DetailsBINDING SITE FOR RESIDUE RET A 201
ChainResidue
ATRP19
AHOH340
AALA33
AGLN38
ACYS53
ATRP58
AASN59
ATRP106
ALYS108
AACT202

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 202
ChainResidue
AVAL62
AGLU72
AGLN97
ATRP106
ARET201
AHOH369

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE RET B 201
ChainResidue
BVAL62
BLYS108

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 202
ChainResidue
BGLU72
BGLN97
BTRP106
BHOH334

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18076076
ChainResidueDetails
ALEU40
ALYS108
BLEU40
BLYS108

218853

PDB entries from 2024-04-24

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