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Ruminococcus bromii AMY12-D392A with maltoheptaose

Analyse Ruminococcus bromii AMY12-D392A with maltoheptaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LSR
Type: protein
Length: 761 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, BGC, CA
Pockets: 7 · best druggability 0.66

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	761	26% helix, 27% strand	A0A2N0UU23

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 7 copies · chains A
BGC · beta-D-glucopyranose · sugar · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.66	0.91	20	GOL
2	212	0.62	0.82	48	GOL
3	285	0.57	0.77	32	BGC, GLC
4	221	0.55	0.78	24	empty
5	57	0.48	0.86	23	GOL

Compared structures

7LSR · Ruminococcus bromii Amy12-D392A 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 7LSR · PDBe 7LSR · UniProt A0A2N0UU23

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