1CSB

Crystal structure of cathepsin b inhibited with CA030 at 2.1 angstroms resolution: A basis for the design of specific epoxysuccinyl inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
B	0006508	biological_process	proteolysis
B	0008234	molecular_function	cysteine-type peptidase activity
D	0006508	biological_process	proteolysis
D	0008234	molecular_function	cysteine-type peptidase activity
E	0006508	biological_process	proteolysis
E	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE EP0 A 48

Chain	Residue
A	GLN23
B	GLY73
B	GLY74
B	HIS110
B	HIS111
B	HIS199
B	TRP221
A	GLY24
A	CYS26
A	GLY27
A	SER28
A	CYS29
A	TRP30
A	HOH267
A	HOH268

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE EP0 E 2

Chain	Residue
D	GLN23
D	GLY24
D	GLY27
D	SER28
D	CYS29
D	TRP30
E	GLY73
E	GLY74
E	HIS110
E	HIS111
E	ALA173
E	GLY198
E	HIS199
E	ALA200
E	TRP221

---

Functional Information from PROSITE/UniProt

site_id	PS00139
Number of Residues	12
Details	THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfGA

Chain	Residue	Details
A	GLN23-ALA34

---

site_id	PS00639
Number of Residues	11
Details	THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRILGWG

Chain	Residue	Details
B	GLY197-GLY207

---

site_id	PS00640
Number of Residues	20
Details	THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvANSWntdWGdnGFFkI

Chain	Residue	Details
B	TYR214-ILE233

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"9299326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10605","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3463996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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