Structure of PDB 4msp Chain B

Receptor sequence
>4mspB (length=189) Species: 9606 (Homo sapiens) [Search protein sequence]
IPEPEVKIEVLQKPFICHRKTKGGDLMLVHYEGYLEKDGSLFHSTHKHNN
GQPIWFTLGILEALKGWDQGLKGMCVGEKRKLIIPPALGYGKEGKGKIPP
ESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWKLSKDEVKAYLKKEFEKH
GAVVNESHHDALVEDIFDKEDEDKDGFISAREFTYKHDE
3D structure
PDB4msp Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y33 F44 H45 L66 Y92 F108
Catalytic site (residue number reindexed from 1) Y31 F42 H43 L64 Y90 F106
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 CA B D129 N131 D133 K135 E140 D127 N129 D131 K133 E138
BS02 CA B D173 D175 D177 F179 E184 D171 D173 D175 F177 E182
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0046872 metal ion binding
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen

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Molecular Function
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Cellular Component
External links
PDB RCSB:4msp, PDBe:4msp, PDBj:4msp
PDBsum4msp
PubMed24272907
UniProtQ9NWM8|FKB14_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP14 (Gene Name=FKBP14)

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