Structure of PDB 5d75 Chain A

Receptor sequence
>5d75A (length=120) Species: 9606 (Homo sapiens) [Search protein sequence]
PKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKN
AKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKI
PPNAKLTFEVELVDIDLEHH
3D structure
PDB5d75 Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.
ChainA
Resolution1.83 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y135 F145 D146 I172 Y198 F216
Catalytic site (residue number reindexed from 1) Y27 F37 D38 I64 Y90 F108
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FK5 A Y135 D146 L162 K170 V171 I172 W175 Y198 Q203 A206 Y27 D38 L54 K62 V63 I64 W67 Y90 Q95 A98 MOAD: Ki=200nM
PDBbind-CN: -logKd/Ki=6.70,Ki=200nM
BS02 JEF A G169 K170 G61 K62
BS03 JEF A P194 E195 G199 K200 K201 N211 P86 E87 G91 K92 K93 N103
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity

View graph for
Molecular Function
External links
PDB RCSB:5d75, PDBe:5d75, PDBj:5d75
PDBsum5d75
PubMed26749369
UniProtQ00688|FKBP3_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP3 (Gene Name=FKBP3)

[Back to BioLiP]