MolNFT v1 · #25046 · protein

Crystal structure of uroporphyrin-III-C-methyltransferase from thermus thermophilus

1VE2 · Uroporphyrin-III C-methyltransferase: “Crystal structure of uroporphyrin-III-C-methyltransferase from thermus thermophilus”. X-ray diffraction, 5 pockets (best druggability 0.77). MolNFT v1 #25046 on GenesisL1: 3D structure, binding…

PDB: 1VE2
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uroporphyrin-III C-methyltransferase
EC: 2.1.1.107
UniProt: Q53WA2
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uroporphyrin-III C-methyltransferase (EC 2.1.1.107)	protein	222	29% helix, 26% strand	Q53WA2
B	Uroporphyrin-III C-methyltransferase (EC 2.1.1.107)	protein	220	33% helix, 26% strand	Q53WA2

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	617	0.77	0.83	62	empty
2	407	0.67	0.80	39	empty
3	297	0.59	0.78	49	empty
4	126	0.44	0.77	31	empty
5	99	0.42	0.78	23	empty

Interfaces

1 interface between chains.

A–B · 2300 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

1VE2 · Crystal structure of uroporphyrin-III-C-methyltransferase from thermus thermophilus · 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 Q53WA2
Elsewhere: RCSB PDB 1VE2 · PDBe 1VE2 · UniProt Q53WA2

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