5VI7

Crystal structure of the Zika virus NS3 helicase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004386	molecular_function	helicase activity
A	0005524	molecular_function	ATP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue SO4 A 701

Chain	Residue
A	PRO196
A	HOH913
A	GLY197
A	GLU286
A	ALA317
A	ARG459
A	ARG462
A	SO4706
A	HOH823
A	HOH830

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 702

Chain	Residue
A	ARG323
A	LYS378
A	ASN568
A	HOH1031
A	HOH1037

---

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 703

Chain	Residue
A	VAL366
A	ARG388
A	THR409
A	HOH829
A	HOH853
A	HOH879
A	HOH955

---

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 A 704

Chain	Residue
A	PRO320
A	GLY321
A	ARG323
A	LYS514
A	HOH821
A	HOH848
A	HOH1015

---

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 705

Chain	Residue
A	ASN463
A	PRO464
A	ASN465
A	ARG588
A	HOH851

---

site_id	AC6
Number of Residues	8
Details	binding site for residue SO4 A 706

Chain	Residue
A	GLY199
A	LYS200
A	THR201
A	ARG202
A	GLU231
A	SO4701
A	HOH809
A	HOH856

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541

Chain	Residue	Details
A	LEU194

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335

Chain	Residue	Details
A	ARG456
A	ARG459

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P06935

Chain	Residue	Details
A	ARG617

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by host => ECO:0000269|PubMed:37478852

Chain	Residue	Details
A	LYS389

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