4XCD

Crystal structure of an octadecameric TF55 complex from S. solfataricus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016853	molecular_function	isomerase activity
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	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016853	molecular_function	isomerase activity
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	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016853	molecular_function	isomerase activity
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	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016853	molecular_function	isomerase activity
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	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016853	molecular_function	isomerase activity
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	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006457	biological_process	protein folding
F	0016853	molecular_function	isomerase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue ADP A 600

Chain	Residue
A	TYR52
A	LEU491
A	VAL504
A	GLU506
A	LYS511
A	GLY53
A	ASP104
A	GLY105
A	LYS107
A	THR108
A	SER173
A	GLY419
A	GLY420

---

site_id	AC2
Number of Residues	12
Details	binding site for residue ADP B 600

Chain	Residue
B	TYR52
B	GLY53
B	PRO54
B	ASP104
B	GLY105
B	LYS107
B	THR108
B	SER173
B	GLY420
B	LEU491
B	VAL504
B	GLU506

---

site_id	AC3
Number of Residues	12
Details	binding site for residue ADP C 600

Chain	Residue
C	TYR52
C	GLY53
C	ASP104
C	GLY105
C	LYS107
C	THR108
C	SER173
C	GLY419
C	GLY420
C	LEU491
C	VAL504
C	LYS511

---

site_id	AC4
Number of Residues	11
Details	binding site for residue ADP D 600

Chain	Residue
D	TYR52
D	GLY53
D	ASP104
D	GLY105
D	LYS107
D	THR108
D	SER173
D	GLY419
D	GLY420
D	LEU491
D	VAL504

---

site_id	AC5
Number of Residues	14
Details	binding site for residue ADP E 600

Chain	Residue
E	TYR52
E	GLY53
E	PRO54
E	ASP104
E	GLY105
E	LYS107
E	THR108
E	SER173
E	GLY419
E	GLY420
E	LEU489
E	LEU491
E	GLU506
E	LYS511

---

site_id	AC6
Number of Residues	12
Details	binding site for residue ADP F 600

Chain	Residue
F	TYR52
F	GLY53
F	ASP104
F	GLY105
F	LYS107
F	THR108
F	SER173
F	GLY419
F	GLY420
F	LEU491
F	VAL504
F	LYS511

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS49-LEU61

---

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

Chain	Residue	Details
A	ILE70-PRO86

---

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

Chain	Residue	Details
A	GLN98-THR106

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6XHI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PDB","id":"6XHJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33682792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6XHJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26853941","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33682792","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---