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Heteroyohimbine synthase THAS1 from catharanthus roseus - apo form

Analyse Heteroyohimbine synthase THAS1 from catharanthus roseus - apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FI5
Type: protein
Length: 684 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetrahydroalstonine synthase
UniProt: A0A0F6SD02
Ligands: ZN, PO4
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tetrahydroalstonine synthase	protein	342	30% helix, 29% strand	A0A0F6SD02

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

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	880	0.75	0.78	71	PO4
2	667	0.74	0.80	49	empty
3	208	0.48	0.75	35	empty
4	77	0.39	0.78	17	empty
5	88	0.36	0.75	19	PO4

Interfaces

1 interface between chains.

A–B · 1309 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

5FI5 · Heteroyohimbine synthase THAS1 from catharanthus roseus - apo form · 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 A0A0F6SD02
Elsewhere: RCSB PDB 5FI5 · PDBe 5FI5 · UniProt A0A0F6SD02

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