5B27

The 1.02A structure of human FABP3 M20S mutant complexed with palmitic acid

PDB DOI: https://doi.org/10.2210/pdb5B27/pdb

Classification: LIPID BINDING PROTEIN
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2016-01-12 Released: 2017-01-18
Deposition Author(s): Matsuoka, D., Sugiyama, S., Kakinouchi, K., Niiyama, M., Murata, M., Matsuoka, S.
Funding Organization(s): JSPS KAKENHI

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.02 Å
R-Value Free: 0.129
R-Value Work: 0.113
R-Value Observed: 0.114

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

The 1.02A structure of human FABP3 M20S mutant complexed with palmitic acid.

Matsuoka, D., Sugiyama, S., Kakinouchi, K., Niiyama, M., Murata, M., Matsuoka, S.

To be published.

Macromolecule Content

Total Structure Weight: 15.29 kDa
Atom Count: 1,617
Modelled Residue Count: 133
Deposited Residue Count: 133
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Fatty acid-binding protein, heart	A	133	Homo sapiens	Mutation(s): 1 Gene Names: FABP3, FABP11, MDGI
UniProt & NIH Common Fund Data Resources
Find proteins for P05413 (Homo sapiens) Explore P05413 Go to UniProtKB: P05413
PHAROS: P05413 GTEx: ENSG00000121769
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P05413
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PLM Query on PLM Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	PALMITIC ACID C₁₆ H₃₂ O₂ IPCSVZSSVZVIGE-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
PG4 Query on PG4 Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	TETRAETHYLENE GLYCOL C₈ H₁₈ O₅ UWHCKJMYHZGTIT-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.02 Å
R-Value Free: 0.129
R-Value Work: 0.113
R-Value Observed: 0.114
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 54.604	α = 90
b = 70.057	β = 90
c = 33.921	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling
MOLREP	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2017-01-18

Deposition Author(s):

Funding Organization	Location	Grant Number
JSPS KAKENHI	Japan	25650051
JSPS KAKENHI	Japan	25286051
JSPS KAKENHI	Japan	24681045
JSPS KAKENHI	Japan	26560436

Revision History (Full details and data files)

Version 1.0: 2017-01-18
Type: Initial release
Version 1.1: 2020-02-26
Changes: Data collection
Version 1.2: 2023-11-08
Changes: Data collection, Database references, Refinement description

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Help and Resources

5B27

The 1.02A structure of human FABP3 M20S mutant complexed with palmitic acid

The 1.02A structure of human FABP3 M20S mutant complexed with palmitic acid.

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)