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Structure of glycinamide-RNase-transformylase T from mycobacterium tuberculosis

Analyse Structure of glycinamide-RNase-transformylase T from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KHR
Type: protein
Length: 669 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Formate-dependent phosphoribosylglycinamide formyltransferase
UniProt: P95197
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Formate-dependent phosphoribosylglycinamide formyltransferase	protein	349	36% helix, 29% strand	P95197
B	Formate-dependent phosphoribosylglycinamide formyltransferase	protein	320	37% helix, 31% strand	P95197

Pockets

6 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	503	0.70	0.80	41	empty
2	101	0.36	0.74	24	empty
3	56	0.34	0.78	13	empty
4	96	0.33	0.73	21	empty
5	86	0.31	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 913 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

6KHR · Structure of glycinamide-RNase-transformylase T from Mycobacterium tuberculosis · 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 P95197
Elsewhere: RCSB PDB 6KHR · PDBe 6KHR · UniProt P95197

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