MolNFT v1 · #31081 · protein
Solution structure of peptidoglycan associated lipoprotein from haemophilus influenza bound to udp-N-acetylmuramoyl-L-alanyl-D- glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
2AIZ · Outer membrane protein P6: “Solution structure of peptidoglycan associated lipoprotein from haemophilus influenza bound to…”. Solution nmr, 2 ligands (UDP, AMU). MolNFT v1 #31081 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2AIZ
- Type
- protein
- Length
- 139 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein P6; Udp-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6…
- UniProt
- P10324
- Ligands
- UDP, AMU
Structure
solution nmr · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Outer membrane protein P6 | protein | 134 | 38% helix, 16% strand | P10324 |
| U | Udp-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6- diaminopimeloyl-D-alanyl-D-alanine | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains P, U
- AMU · N-acetyl-beta-muramic acid · ligand · chains U
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- P–U · 302 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 d-amino, 1 covalent, 1 modified (D-amino acid, covalent ligand, nonstandard).
Compared structures
- 2AIZ · Solution structure of peptidoglycan associated lipoprotein from Haemophilus influenza… · the same entry in another collection · chain P against P, TM-score 1.00
- P10324 · AlphaFold monomer V2.0 prediction for peptidoglycan-associated lipoprotein (P10324) · a predicted model of the same protein · chain P against A, TM-score 0.83
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 P10324
- Elsewhere: RCSB PDB 2AIZ · PDBe 2AIZ · UniProt P10324
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