MolNFT v1 · #181962 · protein

Crystal structure of a single-chain E/F type bilin lyase-isomerase mpeq

7MC4: “Crystal structure of a single-chain E/F type bilin lyase-isomerase mpeq”. X-ray diffraction, 8 pockets (best druggability 0.64). MolNFT v1 #181962 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7MC4
Type: protein
Length: 808 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bilin lyase-isomerase
UniProt: U3MW57
Pockets: 8 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bilin lyase-isomerase	protein	403	72% helix, 0% strand	U3MW57
B	Bilin lyase-isomerase	protein	405	71% helix, 0% strand	U3MW57

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	308	0.64	0.80	42	empty
2	51	0.38	0.81	11	empty
3	60	0.37	0.79	20	empty
4	94	0.37	0.75	18	empty
5	65	0.33	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 609 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

7MC4 · Crystal structure of a single-chain E/F type bilin lyase-isomerase MpeQ · 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 U3MW57
Elsewhere: RCSB PDB 7MC4 · PDBe 7MC4 · UniProt U3MW57

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