1KHQ: Papain

Orthorhombic form of papain/zlfg-dam covalent complex. Determined by X-ray diffraction at 1.6 Å resolution. Released 9 Sept 2003.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Carica papaya
Chains
2
Atoms
1,803
Mol. weight
23.96 kDa
Released
9 Sept 2003

Explore 1KHQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KHQ contains 8 α-helices and 19 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand5-621
α-helix14-163
β-strand1812
β-strand2313
α-helix25-4218
β-strand4814
α-helix50-567
β-strand6413
β-strand6615
α-helix68-7710
β-strand8016
β-strand8214
β-strand10516
β-strand109-11241
α-helix113-1142
α-helix118-12710
β-strand130-13451
α-helix139-1424
β-strand148-14921
β-strand159-16791
β-strand170-17451
β-strand17712
β-strand18311
β-strand186-19051
α-helix199-2013
β-strand207-21041
Chain I: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand25215

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PapainAprotein212Carica papayaP00784 (AlphaFold model)
peptidic inhibitorIprotein5
Sequence of entity 1 (A), FASTA
>1KHQ_1 Papain (chains A)
IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRS
YGCNGGYPWSALQLVAQYGIHYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGA
LLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHAVAAVGYGPNYILIKNSWGTG
WGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
Sequence of entity 2 (I), FASTA
>1KHQ_2 peptidic inhibitor (chains I)
XLFGX

Primary citation

Two polymorphs of a covalent complex between papain and a diazomethylketone inhibitor. Janowski, R., Kozak, M., Jankowska, E. et al. J Pept Res (2004) 64:141-150. DOI 10.1111/j.1399-3011.2004.00181.x · PubMed

Other PDB entries of the same protein (UniProt P00784 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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