Research workbench
Crystal structure of the metallo-beta-lactamase L1 from stenotrophomonas maltophilia in the complex with the hydrolyzed moxalactam and two copper ions
Analyse Crystal structure of the metallo-beta-lactamase L1 from stenotrophomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U2Z
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative metallo-beta-lactamase L1 (beta-lactamase type II) (ec 3.5.2.6) (penicillinase)
- EC
- 3.5.2.6
- UniProt
- B2FTM1
- Ligands
- 3P7, CU
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative metallo-beta-lactamase L1 (beta-lactamase type II) (ec 3.5.2.6) (penicillinase) (EC 3.5.2.6) | protein | 266 | 31% helix, 24% strand | B2FTM1 |
Ligands and binding sites
- 3P7 · (2R)-2-[(1R)-1-{[(2R)-2-carboxy-2-(4-hydroxyphenyl)acetyl]amino}-1-methoxy-2-oxoethyl]-5-methylidene-5,6-dihydro-2H-1,3 -oxazine-4-carboxylic acid · ligand · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.41 | 0.75 | 28 | 3P7, CU |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6U2Z · Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia in… · 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 B2FTM1
- Elsewhere: RCSB PDB 6U2Z · PDBe 6U2Z · UniProt B2FTM1
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