MolNFT v1 · #160859 · protein

Structure of CPGH84D

6PWI · Putative hyaluronoglucosaminidase: “Structure of CPGH84D”. X-ray diffraction, 17 pockets (best druggability 0.74). MolNFT v1 #160859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6PWI
Type: protein
Length: 1,193 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative hyaluronoglucosaminidase
UniProt: A0A0H2YV83
Pockets: 17 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative hyaluronoglucosaminidase	protein	596	43% helix, 17% strand	A0A0H2YV83
B	Putative hyaluronoglucosaminidase	protein	597	43% helix, 16% strand	A0A0H2YV83

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 13 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	790	0.74	0.79	57	empty
2	344	0.57	0.76	36	empty
3	131	0.55	0.82	22	EDO
4	124	0.54	0.82	24	EDO
5	90	0.54	0.84	22	empty

Interfaces

1 interface between chains.

A–B · 858 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6PWI · Structure of CpGH84D · 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 A0A0H2YV83
Elsewhere: RCSB PDB 6PWI · PDBe 6PWI · UniProt A0A0H2YV83

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