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Structure of bacterial enzyme

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

PDB: 4IT9
Type: protein
Length: 904 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Succinate-semialdehyde dehydrogenase
UniProt: B1XMM6
Ligands: PO4
Pockets: 9 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Succinate-semialdehyde dehydrogenase	protein	452	45% helix, 21% strand	B1XMM6

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 31 copies · chains A, B

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

Pockets

9 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	1089	0.84	0.85	121	EDO
2	148	0.66	0.87	26	EDO
3	269	0.65	0.82	42	EDO
4	322	0.61	0.78	43	EDO, PO4
5	337	0.59	0.77	46	EDO, PO4

Interfaces

1 interface between chains.

A–B · 2409 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

4IT9 · Structure of Bacterial Enzyme · 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 B1XMM6
Elsewhere: RCSB PDB 4IT9 · PDBe 4IT9 · UniProt B1XMM6

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