3TNX

Structure of the precursor of a thermostable variant of papain at 2.6 Angstroem resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005764	cellular_component	lysosome
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0097655	molecular_function	serpin family protein binding
C	0004197	molecular_function	cysteine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005615	cellular_component	extracellular space
C	0005764	cellular_component	lysosome
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
C	0051603	biological_process	proteolysis involved in protein catabolic process
C	0097655	molecular_function	serpin family protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 320

Chain	Residue
A	ASN191
A	THR192
A	CYS260

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL264-GLY274

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

Chain	Residue	Details
A	TYR277-ILE296

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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	ALA132
C	ALA132

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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	HIS266
C	HIS266

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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	ASN282
C	ASN282

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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	ALA132
C	ALA132

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 174

Chain	Residue	Details
A	GLN126	electrostatic stabiliser, hydrogen bond donor
A	ALA132	electrostatic stabiliser
A	HIS266	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN282	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	GLN126	electrostatic stabiliser, hydrogen bond donor
C	ALA132	electrostatic stabiliser
C	HIS266	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASN282	activator, electrostatic stabiliser, hydrogen bond acceptor

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