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Ruminococcus bromii AMY12 with maltoheptaose

Analyse Ruminococcus bromii AMY12 with maltoheptaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LSA
Type: protein
Length: 760 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pullulanase
EC: 3.2.1.41
UniProt: A0A2N0UU23
Ligands: GLC, CA
Pockets: 8 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pullulanase (EC 3.2.1.41)	protein	760	26% helix, 27% strand	A0A2N0UU23

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · 8 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	83	0.65	0.91	21	GOL
2	169	0.60	0.83	42	GOL
3	219	0.54	0.78	30	GOL
4	213	0.52	0.77	31	GLC
5	59	0.50	0.86	22	GOL

Compared structures

7LSA · Ruminococcus bromii Amy12 with maltoheptaose · 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 A0A2N0UU23
Elsewhere: RCSB PDB 7LSA · PDBe 7LSA · UniProt A0A2N0UU23

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