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Crystal structure of putative carboxynorspermidine decarboxylase protein from sinorhizobium meliloti

Analyse Crystal structure of putative carboxynorspermidine decarboxylase protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MT1
Type
protein
Length
694 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative carboxynorspermidine decarboxylase protein
EC
4.1.1.-
UniProt
Q92TG9
Ligands
SO4
Pockets
9 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative carboxynorspermidine decarboxylase protein (EC 4.1.1.-)protein34635% helix, 25% strandQ92TG9
BPutative carboxynorspermidine decarboxylase protein (EC 4.1.1.-)protein34835% helix, 24% strandQ92TG9

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11190.710.9224empty
24680.670.7958SO4
33840.630.7850SO4
41240.520.8128empty
5680.510.8523empty

Interfaces

1 interface between chains.

  • A–B · 3076 Ų buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 21 modified (engineered).

Compared structures

  • 3MT1 · Crystal structure of putative carboxynorspermidine decarboxylase protein from… · the same entry in another collection · chain B against B, TM-score 1.00

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