SHEET THE DIMER INTERFACE IS COMPOSED OF INTERDIGITATED N- AND C-TERMINI FROM BOTH SUBUNITS FORMING ...SHEET THE DIMER INTERFACE IS COMPOSED OF INTERDIGITATED N- AND C-TERMINI FROM BOTH SUBUNITS FORMING A FOUR-STRANDED ANTIPARALLEL BETA-SHEET. BECAUSE OF LIMITATIONS IMPOSED BY THE PROTEIN DATA BANK FORMAT IT IS NOT POSSIBLE TO PRESENT THIS SHEET ON SHEET RECORDS. INSTEAD THIS SHEET IS SPECIFIED IN THIS REMARK. STRANDS 1 AND 3 ARE FROM THE MOLECULE IN THIS ENTRY AND STRANDS 2 AND 4 ARE FROM THE SYMMETRY RELATED MOLECULE. I 4 PRO 1 THR 4 0 I 4 THR 96 PHE 99 -1 I 4 THR 96 PHE 99 -1 I 4 PRO 1 THR 4 -1
1: THE EPN INHIBITOR IS COVALENTLY BOUND TO OD2 OF ASP 25.
Components on special symmetry positions
ID
モデル
要素
1
1
A-301-
HOH
詳細
THE HIV-1 PROTEASE IS A DIMER. IN THE CRYSTAL THE TWO MONOMERS ARE RELATED BY A CRYSTALLOGRAPHIC TWO-FOLD AXIS. TO GENERATE THE SYMMETRY RELATED MONOMER, THE FOLLOWING TRANSFORMATION MUST BE APPLIED TO THE COORDINATES PRESENTED IN THIS ENTRY MTRIX1 1 1.000000 0.000000 0.000000 0.000000 MTRIX2 1 0.000000 -1.000000 0.000000 0.000000 MTRIX3 1 0.000000 0.000000 -1.000000 0.000000
THE OCCUPANCY OF THE LIGAND, EPNP, WAS REFINED TO 0.5. THE STOICHIOMETRY OF BINDING OF EPNP TO SIV ...THE OCCUPANCY OF THE LIGAND, EPNP, WAS REFINED TO 0.5. THE STOICHIOMETRY OF BINDING OF EPNP TO SIV PROTEASE IS ONE MOLECULE PER PROTEASE DIMER; ONLY ONE OF THE ACTIVE-SITE ASPARTIC ACIDS PER DIMER BECOMES LABELLED BY EPNP. UPON EPNP BINDING TO THE DIMER, EACH INDIVIDUAL DIMER MOLECULE IS NO LONGER TWO-FOLD SYMMETRICAL AROUND THE CRYSTALLOGRAPHIC TWO-FOLD AXIS. THE DIMER TWO-FOLD IS STILL A CRYSTALLOGRAPHIC TWO-FOLD BECAUSE STATISTICALLY THROUGHOUT THE CRYSTAL THE EPNP IS LOCATED ON EITHER OF THE TWO ACTIVE-SITE ASPARTIC ACIDS WITH EQUAL PROBABILITY.
配列の詳細
SEQUENCE ADVISORY NOTICE DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: POL_ ...SEQUENCE ADVISORY NOTICE DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: POL_SIVM1 SWISS-PROT RESIDUE PDB SEQRES NAME NUMBER NAME CHAIN SEQ/INSERT CODE SER 109 HIS 4 ARG 112 LYS 7 LEU 204 PHE 99 THE SEQUENCE IN THIS ENTRY IS FROM SIVMM239 (AS NAMED IN THE "HUMAN RETROVIRUS AND AIDS" LISTING OF SEQUENCES OF HIV GENOMES, PUBLISHED BY LOS ALAMOS NATIONAL LABORATORY. THIS SEQUENCE IS DIFFERENT THAN THE POL_SIVM1 SEQUENCE ABOVE IN TWO POSITIONS, AT RESIDUE 7 WHICH IS LYS IN THIS STRUCTURE AND ARG IN POL_SIVM1 AND AT RESIDUE 99 WHICH IS PHE IN THIS STRUCTURE AND LEU IN POL_SIMV1. THE HIS AT POSITION 4 IN THIS STRUCTURE IS A POINT MUTANT AND IS A SER IN THE WILD-TYPE SIVMM239 SEQUENCE. THIS POINT MUTATION AT RESIDUE 4 WAS ENGINEERED TO DECREASE THE PROTEASE'S SUSCEPTIBILITY TO AUTOPROTEOLYSIS.
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実験情報
-
実験
実験
手法: X線回折
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試料調製
結晶
マシュー密度: 2.25 Å3/Da / 溶媒含有率: 45.28 %
結晶化
*PLUS
pH: 6.5 / 手法: 蒸気拡散法, ハンギングドロップ法 / 詳細: using macroseeding