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Crystal structure of TTHA1623 from thermus thermophilus HB8

Analyse Crystal structure of TTHA1623 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZWR
Type: protein
Length: 407 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo-beta-lactamase superfamily protein
UniProt: Q5SHV7
Ligands: ZN
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo-beta-lactamase superfamily protein	protein	200	28% helix, 28% strand	Q5SHV7
B	Metallo-beta-lactamase superfamily protein	protein	207	27% helix, 24% strand	Q5SHV7

Ligands and binding sites

ZN · Zinc ion · metal · 14 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.45	0.78	21	empty
2	115	0.40	0.75	31	empty
3	99	0.38	0.75	19	empty
4	101	0.38	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 308 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2ZWR · Crystal structure of TTHA1623 from thermus thermophilus HB8 · 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 Q5SHV7
Elsewhere: RCSB PDB 2ZWR · PDBe 2ZWR · UniProt Q5SHV7

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