MolNFT v1 · #21365 · protein

Crystal structure of HIABD1

1S7M: “Crystal structure of HIABD1”. X-ray diffraction, 10 pockets (best druggability 0.80). MolNFT v1 #21365 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1S7M
Type: protein
Length: 944 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hia
UniProt: Q48152
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 11% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hia	protein	158	10% helix, 45% strand	Q48152
B, E, F	Hia	protein	157	10% helix, 45% strand	Q48152
C	Hia	protein	157	14% helix, 44% strand	Q48152
D	Hia	protein	158	9% helix, 45% strand	Q48152

Pockets

10 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	128	0.80	0.98	22	empty
2	122	0.79	0.97	21	empty
3	843	0.68	0.75	67	empty
4	83	0.35	0.76	20	empty
5	65	0.34	0.77	15	empty

Interfaces

9 interfaces between chains.

A–C · 2816 Å² buried · 60 hydrogen bonds · protein-protein
D–E · 2762 Å² buried · 64 hydrogen bonds · protein-protein
D–F · 2747 Å² buried · 51 hydrogen bonds · protein-protein
B–C · 2721 Å² buried · 55 hydrogen bonds · protein-protein
A–B · 2719 Å² buried · 61 hydrogen bonds · protein-protein

Compared structures

1S7M · Crystal Structure of HiaBD1 · 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 Q48152
Elsewhere: RCSB PDB 1S7M · PDBe 1S7M · UniProt Q48152

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