Research workbench

S.ENTERICA hisa mutant D10G, DUP13-15, Q24L, G102A

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

PDB: 5AC6
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1-(5-phosphoribosyl)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENE amino] imidazole-4-carboxamide…
EC: 5.3.1.16
UniProt: V7IJE3
Ligands: SO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1-(5-phosphoribosyl)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENE amino] imidazole-4-carboxamide isomerase (EC 5.3.1.16)	protein	241	41% helix, 27% strand	V7IJE3

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	428	0.71	0.82	50	SO4

Compared structures

5AC6 · S.enterica HisA mutant D10G, dup13-15, Q24L, G102A · 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 5AC6 · PDBe 5AC6 · UniProt V7IJE3

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