5W74

Crystal Structure of the Group II Chaperonin from Methanococcus Maripaludis D386ADeltaLid Mutant in the Open, ADP-Bound State

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005832	cellular_component	chaperonin-containing T-complex
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005832	cellular_component	chaperonin-containing T-complex
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005832	cellular_component	chaperonin-containing T-complex
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005832	cellular_component	chaperonin-containing T-complex
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005832	cellular_component	chaperonin-containing T-complex
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0005832	cellular_component	chaperonin-containing T-complex
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0005832	cellular_component	chaperonin-containing T-complex
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0000166	molecular_function	nucleotide binding
H	0005524	molecular_function	ATP binding
H	0005832	cellular_component	chaperonin-containing T-complex
H	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue ADP A 600

Chain	Residue
A	LEU39
A	GLY405
A	LEU473
A	ASN474
A	VAL488
A	GLU490
A	LYS495
A	MG601
A	GLY40
A	ASP91
A	GLY92
A	THR94
A	THR95
A	GLY160
A	GLY403
A	GLY404

---

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 601

Chain	Residue
A	THR94
A	ADP600

---

site_id	AC3
Number of Residues	14
Details	binding site for residue ADP B 600

Chain	Residue
B	LEU39
B	ASP91
B	GLY92
B	THR93
B	THR94
B	THR95
B	THR156
B	GLY160
B	GLY403
B	GLY404
B	VAL488
B	GLU490
B	LYS495
B	MG601

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MG B 601

Chain	Residue
B	ASP91
B	ADP600

---

site_id	AC5
Number of Residues	17
Details	binding site for residue ADP C 600

Chain	Residue
C	THR38
C	LEU39
C	GLY40
C	PRO41
C	ASP91
C	GLY92
C	THR93
C	THR94
C	THR95
C	THR156
C	THR159
C	GLY160
C	GLY404
C	LEU473
C	PHE476
C	GLU490
C	MG601

---

site_id	AC6
Number of Residues	3
Details	binding site for residue MG C 601

Chain	Residue
C	ASP91
C	SER157
C	ADP600

---

site_id	AC7
Number of Residues	14
Details	binding site for residue ADP D 600

Chain	Residue
D	LEU39
D	GLY40
D	PRO41
D	ASP91
D	GLY92
D	THR93
D	THR94
D	THR95
D	THR156
D	GLY160
D	GLY404
D	GLU490
D	LYS495
D	MG601

---

site_id	AC8
Number of Residues	3
Details	binding site for residue MG D 601

Chain	Residue
D	ASP91
D	SER157
D	ADP600

---

site_id	AC9
Number of Residues	15
Details	binding site for residue ADP E 600

Chain	Residue
E	LEU39
E	GLY40
E	PRO41
E	ASP91
E	GLY92
E	THR94
E	THR95
E	GLY160
E	GLY403
E	GLY404
E	GLY405
E	LEU473
E	GLU490
E	LYS495
E	MG601

---

site_id	AD1
Number of Residues	2
Details	binding site for residue MG E 601

Chain	Residue
E	ASP91
E	ADP600

---

site_id	AD2
Number of Residues	17
Details	binding site for residue ADP F 600

Chain	Residue
F	GLY404
F	LEU473
F	PHE476
F	GLU490
F	LYS495
F	MG601
F	THR38
F	LEU39
F	GLY40
F	PRO41
F	ASP91
F	GLY92
F	THR94
F	THR95
F	THR156
F	GLY160
F	GLY403

---

site_id	AD3
Number of Residues	3
Details	binding site for residue MG F 601

Chain	Residue
F	ASP91
F	SER157
F	ADP600

---

site_id	AD4
Number of Residues	15
Details	binding site for residue ADP G 600

Chain	Residue
G	LEU39
G	GLY40
G	PRO41
G	ASP91
G	GLY92
G	THR94
G	THR95
G	GLY160
G	GLY403
G	GLY404
G	LEU473
G	VAL488
G	GLU490
G	LYS495
G	MG601

---

site_id	AD5
Number of Residues	2
Details	binding site for residue MG G 601

Chain	Residue
G	ASP91
G	ADP600

---

site_id	AD6
Number of Residues	18
Details	binding site for residue ADP H 600

Chain	Residue
H	THR38
H	LEU39
H	GLY40
H	PRO41
H	ASP91
H	GLY92
H	THR93
H	THR94
H	THR95
H	THR156
H	THR159
H	GLY160
H	GLY404
H	PHE476
H	VAL488
H	GLU490
H	LYS495
H	MG601

---

site_id	AD7
Number of Residues	3
Details	binding site for residue MG H 601

Chain	Residue
H	ASP91
H	SER157
H	ADP600

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG36-LEU48

---

site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP

Chain	Residue	Details
A	VAL57-PRO73

---

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

Chain	Residue	Details
A	GLN85-THR93

---