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Crystal structure of dendranthema morifolium dmat, seleno- methionine derivative

Analyse Crystal structure of dendranthema morifolium dmat, seleno- methionine derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E1V
Type: protein
Length: 880 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl transferase
EC: 2.-.-.-
UniProt: A4PHY4
Pockets: 12 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acyl transferase (EC 2.-.-.-)	protein	440	38% helix, 26% strand	A4PHY4

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	607	0.85	0.90	103	empty
2	607	0.85	0.89	95	empty
3	128	0.79	0.97	22	empty
4	152	0.77	0.94	28	empty
5	208	0.63	0.83	35	empty

Interfaces

1 interface between chains.

A–B · 1757 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified, 2 disulfide (engineered, disulfide).

Compared structures

2E1V · Crystal structure of Dendranthema morifolium DmAT, seleno-methionine derivative · 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 A4PHY4
Elsewhere: RCSB PDB 2E1V · PDBe 2E1V · UniProt A4PHY4

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