Research workbench
MT1-mmp hpx domain with blade 4 loop bound to nanodiscs
Analyse MT1-mmp hpx domain with blade 4 loop bound to nanodiscs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CLZ
- Type
- protein
- Length
- 618 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50281, P02647
- Ligands
- PX4, NA, CL
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 196 | — | P50281 |
| B, C | — | protein | 211 | — | P02647 |
Ligands and binding sites
- PX4 · 1,2-dimyristoyl-sn-glycero-3-phosphocholine · ligand · 218 copies · chains A, B, C
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CLZ · MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs · the same entry in another collection · chain A against A, TM-score 1.00
- P50281 · AlphaFold monomer V2.0 prediction for matrix metalloproteinase-14 (P50281) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P02647 · AlphaFold monomer V2.0 prediction for apolipoprotein a-I (P02647) · a predicted model of the same protein · chain B against A, TM-score 0.51
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 P50281
- Every structure of UniProt P02647
- Elsewhere: RCSB PDB 6CLZ · PDBe 6CLZ · UniProt P50281 · UniProt P02647
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