MolNFT v1 · #178101 · protein

Crystal structure of sah-bound MTA1-P1-P2 complex

7F4N · Transmembrane protein, putative: “Crystal structure of sah-bound MTA1-P1-P2 complex”. X-ray diffraction, 1 ligand (SAH), 8 pockets (best druggability 0.54). MolNFT v1 #178101 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7F4N
Type: protein
Length: 752 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transmembrane protein, putative; Mt-A70 family protein; P1 protein
UniProt: I7M8B9, Q22GC0, Q22VV9
Ligands: SAH
Pockets: 8 · best druggability 0.54

Structure

x-ray diffraction · 6 distinct chains · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Transmembrane protein, putative	protein	130	52% helix, 5% strand	I7M8B9
C	Mt-A70 family protein	protein	215	33% helix, 20% strand	Q22GC0
D	Mt-A70 family protein	protein	216	31% helix, 19% strand	Q22GC0
E	P1 protein	protein	37	65% helix, 0% strand	Q22VV9
F	P1 protein	protein	25	80% helix, 0% strand	Q22VV9
G	Transmembrane protein, putative	protein	129	53% helix, 5% strand	I7M8B9

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains C, D

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

Pockets

8 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	165	0.54	0.80	28	SAH
2	159	0.46	0.76	23	empty
3	143	0.46	0.77	28	SAH
4	153	0.44	0.75	19	empty
5	83	0.38	0.76	16	empty

Interfaces

7 interfaces between chains.

B–C · 1757 Å² buried · 17 hydrogen bonds · protein-protein
D–G · 1743 Å² buried · 21 hydrogen bonds · protein-protein
D–E · 1107 Å² buried · 10 hydrogen bonds · protein-protein
C–F · 860 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 774 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

7F4N · Crystal structure of SAH-bound MTA1-p1-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
Every structure of UniProt Q22VV9
Elsewhere: RCSB PDB 7F4N · PDBe 7F4N · UniProt I7M8B9 · UniProt Q22GC0 · UniProt Q22VV9

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