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Crystal structure of a PMS2 variant

Analyse Crystal structure of a PMS2 variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MFQ
Type: protein
Length: 605 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mismatch repair endonuclease PMS2
EC: 3.1.-.-
UniProt: P54278
Pockets: 9 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mismatch repair endonuclease PMS2 (EC 3.1.-.-)	protein	303	38% helix, 26% strand	P54278
B	Mismatch repair endonuclease PMS2 (EC 3.1.-.-)	protein	302	38% helix, 26% strand	P54278

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.70	0.97	29	empty
2	281	0.66	0.82	35	empty
3	205	0.60	0.81	35	empty
4	198	0.59	0.81	25	empty
5	289	0.58	0.78	36	empty

Interfaces

1 interface between chains.

A–B · 1141 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

6MFQ · Crystal structure of a PMS2 variant · the same entry in another collection · chain A against A, TM-score 1.00
P54278 · AlphaFold monomer V2.0 prediction for mismatch repair endonuclease PMS2 (P54278) · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P54278
Elsewhere: RCSB PDB 6MFQ · PDBe 6MFQ · UniProt P54278

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