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Crystal structure of archaemetzincin (amza) from methanopyrus kandleri at 1.5 a resolution

Analyse Crystal structure of archaemetzincin (amza) from methanopyrus kandleri at 1.5 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X7M
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Archaemetzincin
EC: 3.-.-.-
UniProt: Q8TXW1
Ligands: ZN
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Archaemetzincin (EC 3.-.-.-)	protein	180	36% helix, 19% strand	Q8TXW1

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.38	0.77	17	empty

Compared structures

2X7M · Crystal structure of Archaemetzincin (amzA) from Methanopyrus kandleri at 1.5 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q8TXW1 · AlphaFold monomer V2.0 prediction for archaemetzincin (Q8TXW1) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q8TXW1
Elsewhere: RCSB PDB 2X7M · PDBe 2X7M · UniProt Q8TXW1

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