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Heteroyohimbine synthase hys from catharanthus roseus - apo form

Analyse Heteroyohimbine synthase hys 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: 5H83
Type: protein
Length: 704 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heteroyohimbine synthase hys
Ligands: ZN
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heteroyohimbine synthase hys	protein	354	31% helix, 28% strand	—
B	Heteroyohimbine synthase hys	protein	350	30% helix, 28% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

5 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	901	0.79	0.81	72	empty
2	995	0.78	0.80	82	empty
3	122	0.46	0.78	23	empty
4	74	0.38	0.78	20	empty
5	51	0.31	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 1263 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5H83 · Heteroyohimbine synthase hys 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
Elsewhere: RCSB PDB 5H83 · PDBe 5H83

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