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Crystal structure of a putative S-adenosylmethionine synthetase from cryptosporidium hominis in complex with S-adenosyl-methionine

Analyse Crystal structure of a putative S-adenosylmethionine synthetase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ODJ
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S-adenosylmethionine synthase
EC: 2.5.1.6
UniProt: Q5CKX0
Ligands: SAM, 3PO, MG
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S-adenosylmethionine synthase (EC 2.5.1.6)	protein	386	33% helix, 26% strand	Q5CKX0

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
3PO · Triphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	181	0.51	0.78	31	empty
2	57	0.43	0.82	20	empty
3	65	0.33	0.77	20	empty

Compared structures

4ODJ · Crystal structure of a putative S-adenosylmethionine synthetase from Cryptosporidium… · 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 Q5CKX0
Elsewhere: RCSB PDB 4ODJ · PDBe 4ODJ · UniProt Q5CKX0

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