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Ligand binding domain 1 and 2 of talaromyces marneffei MP1 protein

Analyse Ligand binding domain 1 and 2 of talaromyces marneffei MP1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6J6F
Type: protein
Length: 622 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein
UniProt: A0A093VKV7
Ligands: NI
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope glycoprotein	protein	312	78% helix, 0% strand	A0A093VKV7
B	Envelope glycoprotein	protein	310	79% helix, 0% strand	A0A093VKV7

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B

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

Pockets

6 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	935	0.79	0.81	85	empty
2	736	0.79	0.83	102	empty
3	626	0.78	0.83	87	empty
4	480	0.74	0.83	65	empty
5	85	0.49	0.83	20	empty

Interfaces

1 interface between chains.

A–B · 1632 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6J6F · Ligand binding domain 1 and 2 of Talaromyces marneffei Mp1 protein · the same entry in another collection · chain B against B, 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 A0A093VKV7
Elsewhere: RCSB PDB 6J6F · PDBe 6J6F · UniProt A0A093VKV7

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