MolNFT v1 · #134804 · protein

Crystal structure of mt-I isolated from bothrops asper venom.

5TFV · Basic phospholipase A2 myotoxin III: “Crystal structure of mt-I isolated from bothrops asper venom.”. X-ray diffraction, 1 pocket (best druggability 0.73). MolNFT v1 #134804 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5TFV
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Basic phospholipase A2 myotoxin III
EC: 3.1.1.4
UniProt: P20474
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Basic phospholipase A2 myotoxin III (EC 3.1.1.4)	protein	122	45% helix, 8% strand	P20474

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	651	0.73	0.79	63	empty

Interfaces

1 interface between chains.

A–B · 641 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

P20474 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 myotoxin I (P20474) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P20474
Elsewhere: RCSB PDB 5TFV · PDBe 5TFV · UniProt P20474

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