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Crystal structure of native B3275, member of mccf family of enzymes

Analyse Crystal structure of native B3275, member of mccf family of enzymes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5F9M
Type: protein
Length: 1,376 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mccc family protein
UniProt: Q734X3
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Mccc family protein	protein	344	33% helix, 21% strand	Q734X3

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	847	0.76	0.80	105	empty
2	1057	0.72	0.76	89	empty
3	419	0.68	0.80	63	empty
4	337	0.66	0.80	40	empty
5	56	0.52	0.88	21	empty

Interfaces

4 interfaces between chains.

B–D · 1200 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1194 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 227 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 43 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5F9M · Crystal structure of native B3275, member of MccF family of enzymes · 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 Q734X3
Elsewhere: RCSB PDB 5F9M · PDBe 5F9M · UniProt Q734X3

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