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The mutant E149C-A182C of deinococcus radiodurans N-acylamino acid racemase

Analyse The mutant E149C-A182C of deinococcus radiodurans N-acylamino acid racemase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GGI
Type: protein
Length: 1,440 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acylamino acid racemase
EC: 5.1.1.10
UniProt: Q9RYA6
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	N-acylamino acid racemase (EC 5.1.1.10)	protein	360	37% helix, 23% strand	Q9RYA6

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	739	0.78	0.82	81	empty
2	742	0.78	0.82	79	empty
3	336	0.73	0.85	35	empty
4	413	0.61	0.76	37	empty
5	326	0.58	0.77	38	empty

Interfaces

3 interfaces between chains.

A–C · 1255 Å² buried · 21 hydrogen bonds · protein-protein
B–D · 1242 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 937 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2GGI · The mutant E149C-A182C of Deinococcus Radiodurans N-acylamino acid racemase · 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 Q9RYA6
Elsewhere: RCSB PDB 2GGI · PDBe 2GGI · UniProt Q9RYA6

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