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Structure determination of umud' by mad phasing of the selenomethionyl protein

Analyse Structure determination of umud' by mad phasing of the selenomethionyl protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UMU
Type: protein
Length: 211 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Umud'
EC: 3.4.21.-
UniProt: P04153
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Umud' (EC 3.4.21.-)	protein	105	10% helix, 38% strand	P04153
B	Umud' (EC 3.4.21.-)	protein	106	10% helix, 38% strand	P04153

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.41	0.78	21	empty
2	89	0.39	0.77	19	empty
3	50	0.29	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 539 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1UMU · Structure determination of umud' by mad phasing of the selenomethionyl protein · 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 P04153
Elsewhere: RCSB PDB 1UMU · PDBe 1UMU · UniProt P04153

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