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Crystal structure of apo PTMU3

Analyse Crystal structure of apo PTMU3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OMP
Type: protein
Length: 712 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PTMU3
UniProt: A0A0A0UVH9
Ligands: MN
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	PTMU3	protein	356	45% helix, 17% strand	A0A0A0UVH9

Ligands and binding sites

MN · Manganese (II) ion · metal · 7 copies · chains A, B
ACT · Acetate ion · additive · 10 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	906	0.80	0.82	57	empty
2	618	0.79	0.84	43	empty
3	232	0.54	0.77	50	ACT
4	137	0.44	0.76	23	empty
5	60	0.36	0.79	12	empty

Interfaces

1 interface between chains.

A–B · 2585 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

6OMP · Crystal structure of apo PtmU3 · the same entry in another collection · chain B against B, TM-score 1.00

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 A0A0A0UVH9
Elsewhere: RCSB PDB 6OMP · PDBe 6OMP · UniProt A0A0A0UVH9

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