MolNFT v1 · #144411 · protein

Structure of proline utilization a (puta) with proline bound in remote sites

6BSN · Bifunctional protein puta: “Structure of proline utilization a (puta) with proline bound in remote sites”. X-ray diffraction, 3 ligands (PRO, FDA, SO4), 20 pockets (best druggability 0.86). MolNFT v1 #144411 on GenesisL1: 3D…

PDB: 6BSN
Type: protein
Length: 1,946 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional protein puta
UniProt: Q89E26
Ligands: PRO, FDA, SO4
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein puta	protein	973	51% helix, 14% strand	Q89E26
B	Bifunctional protein puta	protein	973	51% helix, 14% strand	Q89E26

Ligands and binding sites

PRO · Proline · ligand · 9 copies · chains A, B
FDA · Dihydroflavine-adenine dinucleotide · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 14 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1057	0.86	0.87	103	PRO, SO4
2	652	0.85	0.89	50	FDA, SO4
3	398	0.84	0.93	39	FDA, SO4
4	550	0.75	0.83	76	PRO, SO4
5	487	0.74	0.83	73	PRO

Interfaces

1 interface between chains.

A–B · 3384 Å² buried · 67 hydrogen bonds · protein-protein

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 Q89E26
Elsewhere: RCSB PDB 6BSN · PDBe 6BSN · UniProt Q89E26

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