CRYSTAL STRUCTURE OF PAPAIN-SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE COMPLEX AT 1.7 ANGSTROMS RESOLUTION: NONCOVALENT BINDING MODE OF A COMMON SEQUENCE OF ENDOGENOUS THIOL PROTEASE INHIBITORS
The structure was published by Yamamoto, A., Tomoo, K., Doi, M., et al., Tsuboi, S., Okamoto, H., and Okada, Y., in 1992 in a paper entitled "Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1992.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely PAPAIN and SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE.
The molecule most likely forms heterodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: