MolNFT v1 · #178104 · protein

Crystal structure of sah-bound MTA1-P2 complex

7F4Q · Transmembrane protein, putative: “Crystal structure of sah-bound MTA1-P2 complex”. X-ray diffraction, 1 ligand (SAH), 3 pockets (best druggability 0.58). MolNFT v1 #178104 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7F4Q
Type: protein
Length: 344 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transmembrane protein, putative; Mt-A70 family protein
UniProt: I7M8B9, Q22GC0
Ligands: SAH
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Transmembrane protein, putative	protein	129	56% helix, 5% strand	I7M8B9
A	Mt-A70 family protein	protein	215	31% helix, 18% strand	Q22GC0

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.58	0.83	24	empty
2	120	0.52	0.82	30	SAH
3	170	0.44	0.74	25	empty

Interfaces

1 interface between chains.

B–A · 1691 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

7F4Q · Crystal structure of SAH-bound MTA1-p2 complex · the same entry in another collection · chain B against B, 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 I7M8B9
Every structure of UniProt Q22GC0
Elsewhere: RCSB PDB 7F4Q · PDBe 7F4Q · UniProt I7M8B9 · UniProt Q22GC0

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