5GRB

Crystal structure of 2C helicase from enterovirus 71 (EV71) bound with ATPgammaS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003724	molecular_function	RNA helicase activity
A	0016887	molecular_function	ATP hydrolysis activity
B	0003723	molecular_function	RNA binding
B	0003724	molecular_function	RNA helicase activity
B	0016887	molecular_function	ATP hydrolysis activity
C	0003723	molecular_function	RNA binding
C	0003724	molecular_function	RNA helicase activity
C	0016887	molecular_function	ATP hydrolysis activity
D	0003723	molecular_function	RNA binding
D	0003724	molecular_function	RNA helicase activity
D	0016887	molecular_function	ATP hydrolysis activity
E	0003723	molecular_function	RNA binding
E	0003724	molecular_function	RNA helicase activity
E	0016887	molecular_function	ATP hydrolysis activity
F	0003723	molecular_function	RNA binding
F	0003724	molecular_function	RNA helicase activity
F	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue AGS A 401

Chain	Residue
A	SER130
A	ARG260
A	PRO131
A	GLY132
A	THR133
A	GLY134
A	LYS135
A	SER136
A	LEU137
A	ASP177

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 402

Chain	Residue
A	CYS270
A	CYS281
A	SER282
A	CYS286
A	HOH502

---

site_id	AC3
Number of Residues	10
Details	binding site for residue AGS B 401

Chain	Residue
B	GLY129
B	PRO131
B	GLY132
B	THR133
B	GLY134
B	LYS135
B	SER136
B	ASP177
B	THR222
B	ASN223

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 402

Chain	Residue
B	CYS270
B	CYS281
B	SER282
B	CYS286

---

site_id	AC5
Number of Residues	7
Details	binding site for residue AGS C 401

Chain	Residue
C	PRO131
C	GLY132
C	THR133
C	GLY134
C	LYS135
C	SER136
C	ASP177

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN C 402

Chain	Residue
C	CYS270
C	CYS281
C	SER282
C	CYS286

---

site_id	AC7
Number of Residues	7
Details	binding site for residue AGS D 401

Chain	Residue
D	GLY132
D	GLY134
D	LYS135
D	SER136
D	PRO159
D	ASP176
D	ASP177

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN D 402

Chain	Residue
D	CYS270
D	CYS281
D	SER282
D	CYS286

---

site_id	AC9
Number of Residues	7
Details	binding site for residue AGS E 401

Chain	Residue
E	GLY132
E	GLY134
E	LYS135
E	SER136
E	LEU137
E	ASP176
E	ASP177

---

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN E 402

Chain	Residue
E	CYS270
E	CYS281
E	SER282
E	CYS286

---

site_id	AD2
Number of Residues	11
Details	binding site for residue AGS F 401

Chain	Residue
A	ARG119
A	THR196
A	ILE320
F	GLY132
F	GLY134
F	LYS135
F	SER136
F	LEU137
F	ASP176
F	ASP177
F	ALA263

---

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN F 402

Chain	Residue
F	CYS270
F	CYS281
F	SER282
F	CYS286

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	96
Details	ZN_FING: C4-type; degenerate => ECO:0000269|DOI:10.1126/sciadv.1602573

Chain	Residue	Details
A	CYS270-CYS286
B	CYS270-CYS286
C	CYS270-CYS286
D	CYS270-CYS286
E	CYS270-CYS286
F	CYS270-CYS286

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00551

Chain	Residue	Details
A	GLY129
B	GLY129
C	GLY129
D	GLY129
E	GLY129
F	GLY129

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|DOI:10.1126/sciadv.1602573

Chain	Residue	Details
A	CYS270
C	CYS281
C	SER282
C	CYS286
D	CYS270
D	CYS281
D	SER282
D	CYS286
E	CYS270
E	CYS281
E	SER282
A	CYS281
E	CYS286
F	CYS270
F	CYS281
F	SER282
F	CYS286
A	SER282
A	CYS286
B	CYS270
B	CYS281
B	SER282
B	CYS286
C	CYS270

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P03301

Chain	Residue	Details
A	GLN329
B	GLN329
C	GLN329
D	GLN329
E	GLN329
F	GLN329

---