Research workbench
Crystal complex of cyclooxygenase-2: (S)-arn-2508 (a dual COX and faah inhibitor)
Analyse Crystal complex of cyclooxygenase-2: (S)-arn-2508 (a dual COX and faah… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W58
- Type
- protein
- Length
- 557 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q05769
- Ligands
- HEM, FF8, NAG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 557 | — | Q05769 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- FF8 · (2S)-2-{2-fluoro-3'-[(hexylcarbamoyl)oxy][1,1'-biphenyl]-4-yl}propanoic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5W58 · Crystal Complex of Cyclooxygenase-2: (S)-ARN-2508 (a dual COX and FAAH inhibitor) · 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 Q05769
- Elsewhere: RCSB PDB 5W58 · PDBe 5W58 · UniProt Q05769
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