› 2ymb

X-ray diffraction
3.4Å resolution

Structures of MITD1

Released:
DOI: 10.2210/pdb2ymb/pdb
PDB entry 2ymb coloured by chain, front view.
PDB entry 2ymb coloured by chain, side view.
PDB entry 2ymb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes.
Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J
Proc Natl Acad Sci U S A 109 17424-9 (2012)
PMID: 23045692

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186734 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
MIT domain-containing protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 257 amino acids
Theoretical weight: 30.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WV92 (Residues: 1-249; Coverage: 100%)
Gene name: MITD1
Sequence domains:
Structure domains:
Charged multivesicular body protein 1a Chains: F, H
Molecule details ›
Chains: F, H
Length: 14 amino acids
Theoretical weight: 1.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HD42 (Residues: 184-196; Coverage: 7%)
Gene names: CHMP1, CHMP1A, KIAA0047, PCOLN3, PRSM1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: I23
Unit cell:
a: 222.046Å b: 222.046Å c: 222.046Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

The many functions of ESCRTs.
Vietri et al. (2020)
13 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)