MolNFT v1 · #174501 · protein

Crystal structure of CA_00311

7BXB · Gdsl-like LIPASE/ACYLHYDROLASE: “Crystal structure of CA_00311”. X-ray diffraction, 1 ligand (PO4), 13 pockets (best druggability 0.85). MolNFT v1 #174501 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7BXB
Type: protein
Length: 1,320 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gdsl-like LIPASE/ACYLHYDROLASE
UniProt: A0A381K2L8
Ligands: PO4
Pockets: 13 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Gdsl-like LIPASE/ACYLHYDROLASE	protein	220	45% helix, 16% strand	A0A381K2L8

Ligands and binding sites

PO4 · Phosphate ion · ion · 15 copies · chains A, F, B, E, C, D

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

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	491	0.85	0.91	60	PO4
2	509	0.84	0.91	58	PO4
3	306	0.78	0.90	31	empty
4	286	0.77	0.89	33	empty
5	247	0.76	0.89	30	empty

Interfaces

15 interfaces between chains.

B–E · 1219 Å² buried · 9 hydrogen bonds · protein-protein
A–F · 1206 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 1191 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 651 Å² buried · 8 hydrogen bonds · protein-protein
A–D · 648 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7BXB · Crystal structure of Ca_00311 · 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 A0A381K2L8
Elsewhere: RCSB PDB 7BXB · PDBe 7BXB · UniProt A0A381K2L8

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