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Methionyl-trnafmet formyltransferase from escherichia COLI

Analyse Methionyl-trnafmet formyltransferase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FMT
Type: protein
Length: 615 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionyl-tRNA fmet formyltransferase
EC: 2.1.2.9
UniProt: P23882
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionyl-tRNA fmet formyltransferase (EC 2.1.2.9)	protein	308	31% helix, 28% strand	P23882
B	Methionyl-tRNA fmet formyltransferase (EC 2.1.2.9)	protein	307	31% helix, 27% strand	P23882

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	617	0.74	0.80	61	empty
2	308	0.60	0.78	31	empty
3	59	0.33	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 607 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1FMT · Methionyl-trnafmet formyltransferase from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P23882 · AlphaFold monomer V2.0 prediction for methionyl-tRNA formyltransferase (P23882) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23882
Elsewhere: RCSB PDB 1FMT · PDBe 1FMT · UniProt P23882

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