MolNFT v1 · #185522 · protein
Structure of an lpmo at 1.13X10^6 gy
7PZ7 · GH61 isozyme a: “Structure of an lpmo at 1.13X10^6 gy”. X-ray diffraction, 3 ligands (AKR, NAG, CU). MolNFT v1 #185522 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PZ7
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GH61 isozyme a
- EC
- 3.2.1.4
- UniProt
- G3XAP7
- Ligands
- AKR, NAG, CU
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GH61 isozyme a (EC 3.2.1.4) | protein | 227 | 11% helix, 33% strand | G3XAP7 |
Ligands and binding sites
- AKR · Acrylic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- CU · Copper (II) ion · metal · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, methylation).
Compared structures
- 7PZ7 · Structure of an LPMO at 1.13x10^6 Gy · 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 G3XAP7
- Elsewhere: RCSB PDB 7PZ7 · PDBe 7PZ7 · UniProt G3XAP7
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