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Crystal structure of L-lysine, L-arginine carboxypeptidase CC2672 from caulobacter crescentus CB15 complexed with N-methyl phosphonate derivative of L-arginine
Analyse Crystal structure of L-lysine, L-arginine carboxypeptidase CC2672 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MTW
- Type
- protein
- Length
- 403 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-arginine carboxypeptidase CC2672
- UniProt
- Q9A4Z9
- Ligands
- M3R, ZN, SO4
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-arginine carboxypeptidase CC2672 | protein | 403 | 36% helix, 24% strand | Q9A4Z9 |
Ligands and binding sites
- M3R · Methyl phosphonated L-Arginine · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · 7 copies · chains A
- GOL · Glycerol · additive · 7 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 933 | 0.81 | 0.83 | 68 | M3R, GOL |
| 2 | 67 | 0.35 | 0.77 | 17 | GOL |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, carboxylation).
Compared structures
- 3MTW · Crystal structure of L-Lysine, L-Arginine carboxypeptidase Cc2672 from Caulobacter… · 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 Q9A4Z9
- Elsewhere: RCSB PDB 3MTW · PDBe 3MTW · UniProt Q9A4Z9
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