1Q3Q

Crystal structure of the chaperonin from Thermococcus strain KS-1 (two-point mutant complexed with AMP-PNP)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 1527

Chain	Residue
A	ASP95
A	ANP1528

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 2527

Chain	Residue
B	ASP95
B	LYS165
B	ANP2528

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 3527

Chain	Residue
C	ASP95
C	LYS165
C	ANP3528

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 4527

Chain	Residue
D	LYS165
D	ANP4528
D	ASP95

---

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP A 1528

Chain	Residue
A	THR42
A	LEU43
A	GLY44
A	PRO45
A	ASP64
A	CYS65
A	GLY94
A	ASP95
A	GLY96
A	THR97
A	THR98
A	THR99
A	THR160
A	THR163
A	ALA410
A	GLY411
A	ILE447
A	LEU451
A	ILE479
A	ILE494
A	GLU496
A	HOH1008
A	HOH1009
A	HOH1106
A	MG1527

---

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ANP B 2528

Chain	Residue
B	THR42
B	LEU43
B	GLY44
B	PRO45
B	GLY94
B	ASP95
B	GLY96
B	THR97
B	THR98
B	THR99
B	THR163
B	ALA410
B	GLY411
B	LEU451
B	ILE479
B	ILE494
B	GLU496
B	HOH2037
B	HOH2048
B	MG2527

---

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ANP C 3528

Chain	Residue
C	THR42
C	LEU43
C	GLY44
C	PRO45
C	ASP64
C	CYS65
C	GLY94
C	ASP95
C	GLY96
C	THR97
C	THR98
C	THR99
C	THR160
C	THR163
C	ALA410
C	GLY411
C	LEU451
C	ILE494
C	GLU496
C	HOH3023
C	HOH3029
C	HOH3042
C	HOH3075
C	MG3527

---

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ANP D 4528

Chain	Residue
D	HOH4076
D	HOH4110
D	MG4527
D	THR42
D	LEU43
D	GLY44
D	PRO45
D	ASP64
D	CYS65
D	GLY94
D	ASP95
D	GLY96
D	THR97
D	THR98
D	THR99
D	ALA410
D	GLY411
D	LEU451
D	ILE479
D	ILE494
D	GLU496
D	HOH4026

---

Functional Information from PROSITE/UniProt

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. RTtLGPkGmdKML

Chain	Residue	Details
A	ARG40-LEU52

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site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QDkeAGDGT

Chain	Residue	Details
A	GLN89-THR97

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 14729342, 9546398

Chain	Residue	Details
A	THR97
A	THR98
A	ASP64
A	ASP393

---

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 14729342, 9546398

Chain	Residue	Details
B	THR98
B	THR97
B	ASP64
B	ASP393

---

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 14729342, 9546398

Chain	Residue	Details
C	THR98
C	THR97
C	ASP64
C	ASP393

---

site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 14729342, 9546398

Chain	Residue	Details
D	THR98
D	THR97
D	ASP64
D	ASP393

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
A	ASP64	electrostatic stabiliser, hydrogen bond acceptor
A	THR97	electrostatic stabiliser, hydrogen bond donor
A	THR98	electrostatic stabiliser, hydrogen bond donor
A	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
B	ASP64	electrostatic stabiliser, hydrogen bond acceptor
B	THR97	electrostatic stabiliser, hydrogen bond donor
B	THR98	electrostatic stabiliser, hydrogen bond donor
B	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
C	ASP64	electrostatic stabiliser, hydrogen bond acceptor
C	THR97	electrostatic stabiliser, hydrogen bond donor
C	THR98	electrostatic stabiliser, hydrogen bond donor
C	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA4
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
D	ASP64	electrostatic stabiliser, hydrogen bond acceptor
D	THR97	electrostatic stabiliser, hydrogen bond donor
D	THR98	electrostatic stabiliser, hydrogen bond donor
D	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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