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Crystal structure of a putative iron-molybdenum cofactor (femo-co) dinitrogenase (TA1041M) from thermoplasma acidophilum dsm 1728 at 1.30 a resolution

Analyse Crystal structure of a putative iron-molybdenum cofactor (femo-co)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RE2
Type: protein
Length: 238 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein TA1041
UniProt: Q9HJC9
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein TA1041	protein	118	26% helix, 30% strand	Q9HJC9
B	Uncharacterized protein TA1041	protein	120	29% helix, 30% strand	Q9HJC9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	259	0.71	0.86	37	empty
2	66	0.34	0.77	18	empty
3	52	0.28	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 476 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2RE2 · Crystal structure of a putative iron-molybdenum cofactor (femo-co) dinitrogenase… · 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 Q9HJC9
Elsewhere: RCSB PDB 2RE2 · PDBe 2RE2 · UniProt Q9HJC9

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