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Crystal structure of hma (MMAA4) from mycobacterium tuberculosis complexed with sinefungin

Analyse Crystal structure of hma (MMAA4) from mycobacterium tuberculosis complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HA5
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methoxy mycolic acid synthase 4
EC: 2.1.1.-
UniProt: Q79FX8
Ligands: SFG
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methoxy mycolic acid synthase 4 (EC 2.1.1.-)	protein	281	48% helix, 14% strand	Q79FX8

Ligands and binding sites

SFG · Sinefungin · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	476	0.76	0.84	55	SFG
2	64	0.30	0.74	16	empty

Compared structures

3HA5 · Crystal structure of HMA (MMAA4) from mycobacterium tuberculosis complexed with sinefungin · the same entry in another collection · chain A against A, TM-score 1.00
Q79FX8 · AlphaFold monomer V2.0 prediction for hydroxymycolate synthase MMAA4 (Q79FX8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q79FX8
Elsewhere: RCSB PDB 3HA5 · PDBe 3HA5 · UniProt Q79FX8

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