1BKF

FK506 BINDING PROTEIN FKBP MUTANT R42K/H87V COMPLEX WITH IMMUNOSUPPRESSANT FK506

PDB DOI: https://doi.org/10.2210/pdb1BKF/pdb

Classification: ISOMERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 1995-10-18 Released: 1996-08-01
Deposition Author(s): Itoh, S., Decenzo, M.T., Livingston, D.J., Pearlman, D.A., Navia, M.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.60 Å
R-Value Work: 0.187
R-Value Observed: 0.187

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.5 of the entry. See complete history.

Literature

Conformation of Fk506 in X-Ray Structures of its Complexes with Human Recombinant Fkbp12 Mutants

Itoh, S., Decenzo, M.T., Livingston, D.J., Pearlman, D.A., Navia, M.A.

(1995) Bioorg Med Chem Lett 5: 1983

Macromolecule Content

Total Structure Weight: 12.57 kDa
Atom Count: 948
Modelled Residue Count: 107
Deposited Residue Count: 107
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
FK506 BINDING PROTEIN	A	107	Homo sapiens	Mutation(s): 2 EC: 5.2.1.8
UniProt & NIH Common Fund Data Resources
Find proteins for P62942 (Homo sapiens) Explore P62942 Go to UniProtKB: P62942
PHAROS: P62942 GTEx: ENSG00000088832
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P62942
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FK5 Query on FK5 Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN C₄₄ H₆₉ N O₁₂ QJJXYPPXXYFBGM-LFZNUXCKSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Binding Affinity Annotations
ID	Source	Binding Affinity
FK5	BindingDB: 1BKF	Ki: 0.4 (nM) from 1 assay(s)
		Kd: min: 0.2, max: 0.4 (nM) from 2 assay(s)
		IC50: min: 2.3, max: 1000 (nM) from 3 assay(s)
		EC50: 0.9 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.60 Å
R-Value Work: 0.187
R-Value Observed: 0.187
Space Group: P 4₂ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 58.36	α = 90
b = 58.36	β = 90
c = 56.04	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
XENGEN	data reduction
X-PLOR	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 1996-08-01

Deposition Author(s):

Livingston, D.J.

Revision History (Full details and data files)

Version 1.0: 1996-08-01
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2018-03-21
Changes: Data collection, Other
Version 1.4: 2021-11-03
Changes: Database references, Derived calculations
Version 1.5: 2024-02-07
Changes: Data collection

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.