1QXP
Crystal Structure of a mu-like calpain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004198 | molecular_function | calcium-dependent cysteine-type endopeptidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006508 | biological_process | proteolysis |
| B | 0004198 | molecular_function | calcium-dependent cysteine-type endopeptidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DRDGNGKLGlvEF |
| Chain | Residue | Details |
| A | ASP587-PHE599 | |
| A | ASP617-MET629 | |
| A | ASP777-PHE789 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP660 | |
| A | ASN663 | |
| B | ASP660 | |
| B | ASN663 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P17655 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN286 | |
| B | SER105 | |
| B | HIS262 | |
| B | ASN286 | |
| A | SER105 | |
| A | HIS262 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
| Chain | Residue | Details |
| A | ASN591 | |
| A | LYS593 | |
| A | GLU598 | |
| A | ASP587 | |
| A | ASP589 | |
| B | ASP587 | |
| B | ASP589 | |
| B | ASN591 | |
| B | LYS593 | |
| B | GLU598 | |
| B | ASP617 | |
| B | ASP619 | |
| B | SER621 | |
| B | SER623 | |
| B | GLU628 | |
| A | ASP617 | |
| A | ASP619 | |
| A | SER621 | |
| A | SER623 | |
| A | GLU628 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07384 |
| Chain | Residue | Details |
| A | THR344 | |
| B | THR344 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0 |
| Chain | Residue | Details |
| A | ALA734 | |
| A | ASP737 | |
| A | GLU739 | |
| A | GLU744 | |
| A | ASP762 | |
| A | ASP850 | |
| B | ALA734 | |
| B | ASP737 | |
| B | GLU739 | |
| B | GLU744 | |
| B | ASP762 | |
| B | ASP850 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0 |
| Chain | Residue | Details |
| A | ASP777 | |
| A | ASP779 | |
| A | GLU788 | |
| A | GLU807 | |
| A | ASP809 | |
| A | SER811 | |
| A | THR813 | |
| A | GLU818 | |
| B | ASP777 | |
| B | ASP779 | |
| B | THR781 | |
| B | LYS783 | |
| B | GLU788 | |
| B | GLU807 | |
| B | ASP809 | |
| B | SER811 | |
| B | THR813 | |
| B | GLU818 | |
| A | THR781 | |
| A | LYS783 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04632 |
| Chain | Residue | Details |
| A | LYS804 | |
| B | LYS804 |
