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Crystal structure of dmpi from archaeoglobus fulgidus determined to 2.37 ångströms resolution

Analyse Crystal structure of dmpi from archaeoglobus fulgidus determined to 2.37… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M20
Type: protein
Length: 175 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-oxalocrotonate tautomerase, putative
EC: 5.3.2.2
UniProt: O29588
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-oxalocrotonate tautomerase, putative (EC 5.3.2.2)	protein	59	37% helix, 25% strand	O29588
B, C	4-oxalocrotonate tautomerase, putative (EC 5.3.2.2)	protein	58	33% helix, 26% strand	O29588

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.54	0.78	23	empty

Interfaces

3 interfaces between chains.

A–B · 622 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 589 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 580 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3M20 · Crystal structure of DmpI from Archaeoglobus fulgidus determined to 2.37 Angstroms… · the same entry in another collection · chain A against A, 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 O29588
Elsewhere: RCSB PDB 3M20 · PDBe 3M20 · UniProt O29588

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