MolNFT v1 · #13967 · protein

Human ALPHA1-tryptase

1LTO · Alpha tryptase I: “Human ALPHA1-tryptase”. X-ray diffraction, 11 pockets (best druggability 0.71). MolNFT v1 #13967 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LTO
Type: protein
Length: 972 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha tryptase I
EC: 3.4.21.59
UniProt: P15157
Pockets: 11 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Alpha tryptase I (EC 3.4.21.59)	protein	243	12% helix, 37% strand	P15157

Pockets

11 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	762	0.71	0.77	87	empty
2	458	0.67	0.78	56	empty
3	330	0.56	0.75	45	empty
4	89	0.36	0.75	16	empty
5	85	0.35	0.75	17	empty

Interfaces

4 interfaces between chains.

A–D · 1094 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 1065 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 542 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 539 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

1LTO · Human alpha1-tryptase · 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 P15157
Elsewhere: RCSB PDB 1LTO · PDBe 1LTO · UniProt P15157

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