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Discovery of a novel structural motif in methionine aminopeptidase from streptococci with possible post-translational modification

Analyse Discovery of a novel structural motif in methionine aminopeptidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KM3
Type: protein
Length: 563 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine aminopeptidase
UniProt: B2IQ22
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine aminopeptidase	protein	286	26% helix, 20% strand	B2IQ22
B	Methionine aminopeptidase	protein	277	23% helix, 19% strand	B2IQ22

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	927	0.82	0.83	80	empty
2	52	0.64	0.95	33	empty
3	95	0.55	0.85	24	empty
4	60	0.40	0.81	13	empty
5	71	0.34	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1183 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

4KM3 · Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with… · 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 B2IQ22
Elsewhere: RCSB PDB 4KM3 · PDBe 4KM3 · UniProt B2IQ22

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