MolNFT v1 · #111861 · protein

Crystal structure of enoyl reductase domain of mlna from the macrolactin biosynthesis cluster from bacillus amyloliquefaciens

4Z38: “Crystal structure of enoyl reductase domain of mlna from the macrolactin biosynthesis cluster from bacillus…”. X-ray diffraction, 1 ligand (FMN), 13 pockets (best druggability 0.83). MolNFT v1 #111861 on GenesisL1: 3D structure…

PDB: 4Z38
Type: protein
Length: 876 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mlna
UniProt: A7Z470
Ligands: FMN
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mlna	protein	437	49% helix, 12% strand	A7Z470
B	Mlna	protein	439	49% helix, 12% strand	A7Z470

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1003	0.83	0.84	108	FMN
2	730	0.83	0.87	74	FMN
3	93	0.64	0.90	20	empty
4	79	0.63	0.91	21	empty
5	138	0.50	0.79	18	empty

Interfaces

1 interface between chains.

A–B · 1885 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4Z38 · Crystal structure of enoyl reductase domain of MlnA from the macrolactin biosynthesis… · 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 A7Z470
Elsewhere: RCSB PDB 4Z38 · PDBe 4Z38 · UniProt A7Z470

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