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Crystal structure of a secreted mycobacterium tuberculosis heme- binding protein

Analyse Crystal structure of a secreted mycobacterium tuberculosis heme- binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MAY
Type: protein
Length: 743 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Possible exported protein
UniProt: O53654
Pockets: 9 · best druggability 0.84

Structure

x-ray diffraction · 7 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, F	Possible exported protein	protein	86	81% helix, 0% strand	O53654
B	Possible exported protein	protein	93	82% helix, 0% strand	O53654
C	Possible exported protein	protein	97	80% helix, 0% strand	O53654
D	Possible exported protein	protein	94	82% helix, 0% strand	O53654
E	Possible exported protein	protein	94	82% helix, 0% strand	O53654
G	Possible exported protein	protein	97	82% helix, 0% strand	O53654
H	Possible exported protein	protein	96	80% helix, 0% strand	O53654

Pockets

9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1087	0.84	0.84	101	empty
2	854	0.84	0.85	74	empty
3	538	0.77	0.83	42	empty
4	483	0.76	0.84	36	empty
5	426	0.73	0.83	37	empty

Interfaces

13 interfaces between chains.

G–H · 1891 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 1878 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 1346 Å² buried · 15 hydrogen bonds · protein-protein
E–F · 1337 Å² buried · 13 hydrogen bonds · protein-protein
E–H · 530 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3MAY · Crystal structure of a secreted Mycobacterium tuberculosis heme-binding protein · 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 O53654
Elsewhere: RCSB PDB 3MAY · PDBe 3MAY · UniProt O53654

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