Structure for peptidase C02.001: calpain-1

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
2ARY Homo sapiens 2.40 Å catalytic domain only
Catalytic residues are shown in ball-and-stick representation: Gln109 and Asn296 in pink, Cys115 in yellow and His272 in purple.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
complex with inhibitor Z-Leu-Leu-Tyr-CH2F 2.00 Å 1ZCM 1ZCM 1ZCM 1ZCM 1ZCM 1ZCM Li et al., 2006
catalytic domain only 2.40 Å 2ARY 2ARY 2ARY 2ARY 2ARY 2ARY Davis et al., 2007
Rattus norvegicus
catalytic domain only 2.07 Å 1KXR 1KXR 1KXR 1KXR 1KXR 1KXR Moldoveanu et al., 2002
mature  peptidase 2.80 Å 1QXP 1QXP 1QXP 1QXP 1QXP 1QXP Pal et al., 2003
protease core; complex with leupeptin 1.80 Å 1TL9 1TL9 1TL9 1TL9 1TL9 1TL9 Moldoveanu et al., 2004
peptidase unit only; complex with E64 1.90 Å 1TLO 1TLO 1TLO 1TLO 1TLO 1TLO Moldoveanu et al., 2004
calpain 1 proteolytic core;ncomplex with snj-1715, a cyclic hemiacetal-type inhibitor 2.25 Å 2G8E 2G8E 2G8E 2G8E 2G8E 2G8E Cuerrier et al., 2006
proteolytic core; complex with snj-1945, a alpha-ketoamide-type inhibitor. 1.61 Å 2G8J 2G8J 2G8J 2G8J 2G8J 2G8J Cuerrier et al., 2006
calpain 1 proteolytic core inactivated by wr18(s,s), an epoxysuccinyl-type inhibitor. 2.04 Å 2NQG 2NQG 2NQG 2NQG 2NQG 2NQG Cuerrier et al., 2007
calpain 1 proteolytic core inactivated by wr13(r,r), an epoxysuccinyl-type inhibitor. 2.04 Å 2NQI 2NQI 2NQI 2NQI 2NQI 2NQI Cuerrier et al., 2007
calpain 1 proteolytic core inactivated by zlak-3001, an alpha-ketoamide 1.80 Å 2R9C 2R9C 2R9C 2R9C 2R9C 2R9C Qian et al., 2008
calpain 1 proteolytic core inactivated by zlak-3002, an alpha-ketoamide 1.60 Å 2R9F 2R9F 2R9F 2R9F 2R9F 2R9F Qian et al., 2008