Download MendeleyCrystal structure of an apoptosis-inducing factor, mitochondrion-associated, 1 (AIFM1) from Homo sapiens at 1.88 A resolution
Joint Center for Structural Genomics (JCSG), Partnership for T-Cell Biology (TCELL)To be published.
4LII
Crystal structure of an apoptosis-inducing factor, mitochondrion-associated, 1 (AIFM1) from Homo sapiens at 1.88 A resolution
- PDB DOI: https://doi.org/10.2210/pdb4LII/pdb
- Classification: OXIDOREDUCTASE, APOPTOSIS
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2013-07-02 Released: 2013-09-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.88 Å
- R-Value Free: 0.211
- R-Value Work: 0.167
- R-Value Observed: 0.169
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Apoptosis-inducing factor 1, mitochondrial | 513 | Homo sapiens | Mutation(s): 0 Gene Names: AIF, AIFM1, BC111065, PDCD8 EC: 1 (PDB Primary Data), 1.6.99 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O95831 (Homo sapiens) Explore O95831 Go to UniProtKB: O95831 | |||||
PHAROS: O95831 GTEx: ENSG00000156709 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O95831 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FAD Query on FAD | B [auth A] | FLAVIN-ADENINE DINUCLEOTIDE C27 H33 N9 O15 P2 VWWQXMAJTJZDQX-UYBVJOGSSA-N |  | ||
| EDO Query on EDO | C [auth A], D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.88 Å
- R-Value Free: 0.211
- R-Value Work: 0.167
- R-Value Observed: 0.169
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M34LII
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 50.68 | α = 90 |
| b = 89.807 | β = 94.78 |
| c = 60.471 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| PDB_EXTRACT | data extraction |
| SHELX | phasing |
| SHARP | phasing |
| XSCALE | data scaling |
| REFMAC | refinement |
| XDS | data reduction |
| SHELXD | phasing |
Entry History
Deposition Data
- Released Date: 2013-09-04 Deposition Author(s): Joint Center for Structural Genomics (JCSG), Partnership for T-Cell Biology (TCELL)
Revision History (Full details and data files)
- Version 1.0: 2013-09-04
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description - Version 1.2: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
