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Crystal structure of riboflavin synthase

Analyse Crystal structure of riboflavin synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1I8D
Type: protein
Length: 592 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Riboflavin synthase
EC: 2.5.1.9
UniProt: P29015
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 22% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Riboflavin synthase (EC 2.5.1.9)	protein	206	23% helix, 42% strand	P29015
B	Riboflavin synthase (EC 2.5.1.9)	protein	201	22% helix, 41% strand	P29015
C	Riboflavin synthase (EC 2.5.1.9)	protein	185	22% helix, 41% strand	P29015

Pockets

7 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	549	0.78	0.85	64	empty
2	618	0.72	0.79	71	empty
3	88	0.35	0.74	16	empty
4	68	0.33	0.76	12	empty
5	75	0.32	0.74	12	empty

Interfaces

3 interfaces between chains.

A–C · 1605 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 765 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 477 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1I8D · Crystal structure of riboflavin synthase · 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 P29015
Elsewhere: RCSB PDB 1I8D · PDBe 1I8D · UniProt P29015

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