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3BXS

Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1 Protease. Implications For Catalytic Mechanism

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, BProteasepolymer9910765.72UniProt (P03369)
Pfam (PF00077)
In PDB
Retropepsin, PR
2A, BSULFATE IONnon-polymer96.13Chemie (SO4)
3A, B(9S,12S)-9-(1-methylethyl)-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxylic acidnon-polymer362.42Chemie (DRS)
4waterwater18.0201Chemie (HOH)
Sequence modifications
A, B: 1 - 99 (UniProt: P03369)
PDBExternal DatabaseDetails
Lys 7Gln 497engineered mutation
Ile 33Leu 523engineered mutation
Aba 67Cys 557engineered mutation
Aba 95Cys 585engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight21531.4
Non-Polymers*Number of molecules5
Total formula weight1013.0
All*Total formula weight22544.4
*Water molecules are not included.

217705

数据于2024-03-27公开中

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