Research workbench

S. enterica hisa mutant D10G, DUP13-15, Q24L, G102A, V106L

Analyse S. enterica hisa mutant D10G, DUP13-15, Q24L, G102A, V106L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5G4E
Type: protein
Length: 426 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
EC: 5.3.1.16
UniProt: V7IJE3
Ligands: NA, SO4
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(EC 5.3.1.16)	protein	220	41% helix, 26% strand	V7IJE3
B	(EC 5.3.1.16)	protein	206	44% helix, 22% strand	V7IJE3

Ligands and binding sites

NA · Sodium ion · metal · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B
ACY · Acetic acid · additive · 2 copies · chains A, B
GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	76	0.75	0.98	22	empty
2	498	0.74	0.83	44	SO4
3	298	0.60	0.78	34	SO4

Interfaces

1 interface between chains.

A–B · 670 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5G4E · S. enterica HisA mutant D10G, Dup13-15, Q24L, G102A, V106L · 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 V7IJE3
Elsewhere: RCSB PDB 5G4E · PDBe 5G4E · UniProt V7IJE3

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