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Crystal structure of thermoplasma acidophilum 1320 (APC5513)

Analyse Crystal structure of thermoplasma acidophilum 1320 (APC5513) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NE2
Type: protein
Length: 360 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TA1320
UniProt: Q9HIL9
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TA1320	protein	176	39% helix, 31% strand	Q9HIL9
B	Hypothetical protein TA1320	protein	184	40% helix, 30% strand	Q9HIL9

Ligands and binding sites

FMT · Formic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.51	0.75	42	empty
2	62	0.32	0.76	16	empty
3	54	0.29	0.75	16	empty
4	51	0.26	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 674 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 2 disulfide (engineered, disulfide).

Compared structures

1NE2 · Crystal Structure of Thermoplasma acidophilum 1320 (APC5513) · 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 Q9HIL9
Elsewhere: RCSB PDB 1NE2 · PDBe 1NE2 · UniProt Q9HIL9

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