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Thermus thermophilus uroporphyrinogen III synthase

Analyse Thermus thermophilus uroporphyrinogen III synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3D8T
Type: protein
Length: 501 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uroporphyrinogen-III synthase
EC: 4.2.1.75
UniProt: Q72KM1
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uroporphyrinogen-III synthase (EC 4.2.1.75)	protein	252	46% helix, 21% strand	Q72KM1
B	Uroporphyrinogen-III synthase (EC 4.2.1.75)	protein	249	44% helix, 18% strand	Q72KM1

Ligands and binding sites

ACT · Acetate ion · additive · 4 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	496	0.63	0.76	58	ACT
2	247	0.63	0.81	33	empty
3	359	0.61	0.77	47	ACT
4	98	0.47	0.81	18	empty

Interfaces

1 interface between chains.

A–B · 699 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3D8T · Thermus thermophilus Uroporphyrinogen III 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 Q72KM1
Elsewhere: RCSB PDB 3D8T · PDBe 3D8T · UniProt Q72KM1

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