3IMA

Complex structure of tarocystatin and papain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
B	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
D	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 300

Chain	Residue
A	ASN18
A	ARG83

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 301

Chain	Residue
A	ARG111
A	GLN112
A	ARG188
A	HOH385

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 300

Chain	Residue
C	LYS17
C	ARG83
C	HOH219

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLN19-ALA30

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site_id	PS00287
Number of Residues	14
Details	CYSTATIN Cysteine proteases inhibitors signature. QQVVSGIMHhLTVE

Chain	Residue	Details
B	GLN48-GLU61

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

Chain	Residue	Details
A	VAL157-GLY167

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

Chain	Residue	Details
A	TYR170-ILE189

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0000305|PubMed:1860874, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP

Chain	Residue	Details
A	OCS25
C	OCS25

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP

Chain	Residue	Details
A	HIS159
C	HIS159

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP

Chain	Residue	Details
A	ASN175
C	ASN175

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: covalent => ECO:0000269|PubMed:8416808, ECO:0007744|PDB:1POP

Chain	Residue	Details
A	OCS25
C	OCS25

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 174

Chain	Residue	Details
A	GLN19	electrostatic stabiliser, hydrogen bond donor
A	OCS25	electrostatic stabiliser
A	HIS159	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN175	activator, electrostatic stabiliser, hydrogen bond acceptor

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 174

Chain	Residue	Details
C	GLN19	electrostatic stabiliser, hydrogen bond donor
C	OCS25	electrostatic stabiliser
C	HIS159	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASN175	activator, electrostatic stabiliser, hydrogen bond acceptor

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