MolNFT v1 · #27773 · protein

Structural analysis of leishmania major LMAJ004091AAA, a SAM-dependent methyltransferase of the DUF858/PFAM05891 family

1XTP: “Structural analysis of leishmania major LMAJ004091AAA, a SAM-dependent methyltransferase of the…”. X-ray diffraction, 1 ligand (SAI), 1 pocket (best druggability 0.76). MolNFT v1 #27773 on GenesisL1: 3D structure, binding sites and…

PDB: 1XTP
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LMAJ004091AAA
UniProt: Q4Q7M2
Ligands: SAI
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LMAJ004091AAA	protein	246	36% helix, 25% strand	Q4Q7M2

Ligands and binding sites

SAI · S-adenosyl-L-homoselenocysteine · ligand · chains A

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	399	0.76	0.85	46	SAI

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

1XTP · Structural Analysis of Leishmania major LMAJ004091AAA, a SAM-dependent methyltransferase… · 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 Q4Q7M2
Elsewhere: RCSB PDB 1XTP · PDBe 1XTP · UniProt Q4Q7M2

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