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	SER105
A	HIS262
A	ASN286
B	SER105
B	HIS262
B	ASN286

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
A	ASP587
A	GLU628
B	ASP587
B	ASP589
B	ASN591
B	LYS593
B	GLU598
B	ASP617
B	ASP619
B	SER621
B	SER623
A	ASP589
B	GLU628
A	ASN591
A	LYS593
A	GLU598
A	ASP617
A	ASP619
A	SER621
A	SER623

---

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
B	GLU744
B	ASP762
B	ASP850
A	ASP737
A	GLU739
A	GLU744
A	ASP762
A	ASP850
B	ALA734
B	ASP737
B	GLU739

---

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	GLU818
B	ASP777
B	ASP779
B	THR781
B	LYS783
B	GLU788
B	GLU807
B	ASP809
B	SER811
B	THR813
A	ASP779
B	GLU818
A	THR781
A	LYS783
A	GLU788
A	GLU807
A	ASP809
A	SER811
A	THR813

---

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

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
A	ASN286
A	HIS262
A	GLN99
A	SER105

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
B	ASN286
B	HIS262
B	GLN99
B	SER105

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
A	ASN286
A	HIS262
A	GLN99
A	SER105
A	TRP288

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
B	ASN286
B	HIS262
B	GLN99
B	SER105
B	TRP288

---