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Structure of a family 2 pectate lyase in complex with a transition metal

Analyse Structure of a family 2 pectate lyase in complex with a transition metal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V8J
Type
protein
Length
535 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pectate lyase
EC
4.2.2.2
Ligands
MN
Pockets
2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APectate lyase (EC 4.2.2.2)protein53543% helix, 14% strand—

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.650.8136empty
24520.640.7738empty

Compared structures

  • 2V8J · Structure of a Family 2 Pectate Lyase in Complex with a Transition Metal · the same entry in another collection · chain A against A, TM-score 1.00

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