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Structure of human mthfs

Analyse Structure of human mthfs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HXT
Type: protein
Length: 195 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-formyltetrahydrofolate cyclo-ligase
EC: 6.3.3.2
UniProt: P49914
Ligands: MG, NI
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2)	protein	195	35% helix, 21% strand	P49914

Ligands and binding sites

MG · Magnesium ion · metal · 7 copies · chains A
NI · Nickel (II) ion · metal · 4 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	109	0.74	0.94	24	NI
2	62	0.39	0.80	18	empty
3	67	0.32	0.75	14	empty

Compared structures

3HXT · Structure of human MTHFS · the same entry in another collection · chain A against A, TM-score 1.00
P49914 · AlphaFold monomer V2.0 prediction for 5-formyltetrahydrofolate cyclo- ligase (P49914) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P49914
Elsewhere: RCSB PDB 3HXT · PDBe 3HXT · UniProt P49914

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