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Crystal structure of HA17-HA33-ipt

Analyse Crystal structure of HA17-HA33-ipt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BP5
Type: protein
Length: 715 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ha-33; Ha-17
UniProt: Q45871, Q45878
Ligands: IPT
Pockets: 6 · best druggability 0.49

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ha-33	protein	286	9% helix, 48% strand	Q45871
C	Ha-17	protein	144	6% helix, 50% strand	Q45878
B	Ha-33	protein	285	9% helix, 46% strand	Q45871

Ligands and binding sites

IPT · 1-methylethyl 1-thio-beta-D-galactopyranoside · ligand · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.49	0.78	23	empty
2	85	0.44	0.80	19	empty
3	114	0.43	0.78	21	empty
4	71	0.41	0.80	18	empty
5	112	0.37	0.73	17	empty

Interfaces

3 interfaces between chains.

A–B · 1011 Å² buried · 14 hydrogen bonds · protein-protein
C–B · 685 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 448 Å² buried · 2 hydrogen bonds · protein-protein

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 Q45871
Every structure of UniProt Q45878
Elsewhere: RCSB PDB 5BP5 · PDBe 5BP5 · UniProt Q45871 · UniProt Q45878

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