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Crystal structure of mtmc in complex with SAM and tdp

Analyse Crystal structure of mtmc in complex with SAM and tdp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RVG
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-mycarose 3-C-methyltransferase
UniProt: Q194Q4
Ligands: TYD, SAM, ZN
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-mycarose 3-C-methyltransferase	protein	418	36% helix, 22% strand	Q194Q4

Ligands and binding sites

TYD · Thymidine-5'-diphosphate · ligand · chains A
SAM · S-adenosylmethionine · ligand · chains A
ZN · Zinc ion · metal · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

2 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	800	0.83	0.86	75	TYD, SAM, ACT
2	65	0.28	0.73	18	empty

Compared structures

4RVG · Crystal structure of MtmC in complex with SAM and TDP · 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 Q194Q4
Elsewhere: RCSB PDB 4RVG · PDBe 4RVG · UniProt Q194Q4

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