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Crystal structure HPIC1 in P42 space group

Analyse Crystal structure HPIC1 in P42 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AL6
Type: protein
Length: 391 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 12-epi-hapalindole C/U synthase
UniProt: A0A076NBW8
Ligands: CA
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	12-epi-hapalindole C/U synthase	protein	194	0% helix, 43% strand	A0A076NBW8
B	12-epi-hapalindole C/U synthase	protein	197	0% helix, 43% strand	A0A076NBW8

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.78	0.95	21	empty
2	119	0.66	0.89	29	empty
3	94	0.65	0.90	26	empty
4	137	0.60	0.84	21	empty
5	199	0.44	0.74	30	empty

Interfaces

1 interface between chains.

A–B · 887 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6AL6 · Crystal structure HpiC1 in P42 space group · 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 A0A076NBW8
Elsewhere: RCSB PDB 6AL6 · PDBe 6AL6 · UniProt A0A076NBW8

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