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Mat in complex with samh

Analyse Mat in complex with samh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OCK
Type
protein
Length
3,666 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S-adenosylmethionine synthase; SAM hydrolase
EC
2.5.1.6
UniProt
A0A4S5B2W6, P07693
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 6 distinct chains · 28% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, C, FS-adenosylmethionine synthase (EC 2.5.1.6)protein38433% helix, 24% strandA0A4S5B2W6
D, E, G, H, IS-adenosylmethionine synthase (EC 2.5.1.6)protein38334% helix, 24% strandA0A4S5B2W6
LSAM hydrolaseprotein15222% helix, 23% strandP07693
ASAM hydrolaseprotein15122% helix, 26% strandP07693
KSAM hydrolaseprotein14719% helix, 29% strandP07693
JSAM hydrolaseprotein14922% helix, 31% strandP07693

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110690.850.86120empty
21740.790.9429empty
38890.790.8290empty
49660.790.81111empty
52390.780.9136empty

Interfaces

21 interfaces between chains.

  • B–C · 2362 Ų buried · 24 hydrogen bonds · protein-protein
  • F–G · 2295 Ų buried · 35 hydrogen bonds · protein-protein
  • D–E · 2188 Ų buried · 23 hydrogen bonds · protein-protein
  • H–I · 2140 Ų buried · 32 hydrogen bonds · protein-protein
  • A–K · 1069 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 7OCK · MAT in complex with SAMH · the same entry in another collection · chain C against C, TM-score 1.00

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