Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GXA

Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003678	molecular_function	DNA helicase activity
A	0005524	molecular_function	ATP binding
A	0006260	biological_process	DNA replication
B	0003677	molecular_function	DNA binding
B	0003678	molecular_function	DNA helicase activity
B	0005524	molecular_function	ATP binding
B	0006260	biological_process	DNA replication
C	0003677	molecular_function	DNA binding
C	0003678	molecular_function	DNA helicase activity
C	0005524	molecular_function	ATP binding
C	0006260	biological_process	DNA replication
D	0003677	molecular_function	DNA binding
D	0003678	molecular_function	DNA helicase activity
D	0005524	molecular_function	ATP binding
D	0006260	biological_process	DNA replication
E	0003677	molecular_function	DNA binding
E	0003678	molecular_function	DNA helicase activity
E	0005524	molecular_function	ATP binding
E	0006260	biological_process	DNA replication
F	0003677	molecular_function	DNA binding
F	0003678	molecular_function	DNA helicase activity
F	0005524	molecular_function	ATP binding
F	0006260	biological_process	DNA replication
G	0003677	molecular_function	DNA binding
G	0003678	molecular_function	DNA helicase activity
G	0005524	molecular_function	ATP binding
G	0006260	biological_process	DNA replication
H	0003677	molecular_function	DNA binding
H	0003678	molecular_function	DNA helicase activity
H	0005524	molecular_function	ATP binding
H	0006260	biological_process	DNA replication
I	0003677	molecular_function	DNA binding
I	0003678	molecular_function	DNA helicase activity
I	0005524	molecular_function	ATP binding
I	0006260	biological_process	DNA replication
J	0003677	molecular_function	DNA binding
J	0003678	molecular_function	DNA helicase activity
J	0005524	molecular_function	ATP binding
J	0006260	biological_process	DNA replication
K	0003677	molecular_function	DNA binding
K	0003678	molecular_function	DNA helicase activity
K	0005524	molecular_function	ATP binding
K	0006260	biological_process	DNA replication
L	0003677	molecular_function	DNA binding
L	0003678	molecular_function	DNA helicase activity
L	0005524	molecular_function	ATP binding
L	0006260	biological_process	DNA replication

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 21

Chain	Residue
A	ADP1
A	SER440
A	ASP479
A	HOH578
A	HOH579
B	HOH3
B	ARG538

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 22

Chain	Residue
B	HOH6
B	SER440
B	ASP479
C	HOH5
C	ARG538
B	ADP2
B	HOH4

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG C 23

Chain	Residue
C	ADP3
C	HOH7
C	HOH8
C	SER440
C	ASP479
D	HOH9
D	ARG538

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 24

Chain	Residue
D	ADP4
D	SER440
D	ASP479
E	TYR534

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 25

Chain	Residue
E	ADP5
E	SER440
E	ASP479

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG G 27

Chain	Residue
G	ADP7
G	HOH10
G	HOH11
G	HOH12
G	SER440
G	ASP479
H	ARG538

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG H 28

Chain	Residue
H	ADP8
H	HOH13
H	HOH14
H	CL48
H	SER440
H	ASP479
I	HOH15
I	ARG538

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG I 29

Chain	Residue
I	SER440
I	ASP479
J	ADP9

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG J 30

Chain	Residue
J	SER440
J	ASP479
K	ADP10

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG K 31

Chain	Residue
K	SER440
K	ASP479
L	ADP11

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 41

Chain	Residue
A	ADP1
A	LYS439
B	ARG538

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 42

Chain	Residue
B	ADP2
B	LYS439
B	ASN523

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL H 48

Chain	Residue
H	ADP8
H	MG28
H	PRO435
H	LYS439
H	ASP479
H	ASN523

site_id	BC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP A 1

Chain	Residue
A	MG21
A	CL41
A	ASN436
A	THR437
A	GLY438
A	LYS439
A	SER440
A	MET441
A	ASN558
A	HOH578
A	HOH579
B	ILE423
B	PRO424
B	LYS425
B	LYS426
B	TYR499

site_id	BC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP B 2

Chain	Residue
B	HOH4
B	MG22
B	CL42
B	ASN436
B	THR437
B	GLY438
B	LYS439
B	SER440
B	MET441
B	ASN558
C	HOH5
C	PRO424
C	LYS425
C	LYS426
C	TYR499

site_id	BC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP C 3

Chain	Residue
C	THR437
C	GLY438
C	LYS439
C	SER440
C	MET441
C	THR549
C	ASN558
D	PRO424
D	LYS425
D	TYR499
C	HOH7
C	HOH8
C	MG23
C	ASN436

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP D 4

Chain	Residue
D	MG24
D	ASN436
D	THR437
D	GLY438
D	LYS439
D	SER440
D	THR549
D	GLN555
E	TYR499
E	TYR534

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ADP E 5

Chain	Residue
E	MG25
E	ASN436
E	THR437
E	GLY438
E	LYS439
E	SER440
E	MET441
F	TYR499

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP F 6

Chain	Residue
F	PRO435
F	ASN436
F	THR437
F	GLY438
F	LYS439
F	SER440
F	MET441
F	ASP479
F	ASN523
F	CYS548
F	PHE557

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP G 7

Chain	Residue
G	HOH10
G	HOH11
G	MG27
G	ASN436
G	THR437
G	GLY438
G	LYS439
G	SER440
G	MET441
G	ASN558
H	LYS425
H	TYR499

site_id	CC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADP H 8

Chain	Residue
H	HOH14
H	MG28
H	CL48
H	ASN436
H	THR437
H	GLY438
H	LYS439
H	SER440
H	MET441
H	ASN558
I	PRO424
I	LYS425
I	TYR499

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ADP J 9

Chain	Residue
I	MG29
I	ASN436
I	THR437
I	GLY438
I	LYS439
I	SER440
I	MET441
I	GLN555
J	TYR499

site_id	CC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP K 10

Chain	Residue
J	MG30
J	ASN436
J	THR437
J	GLY438
J	LYS439
J	SER440
J	MET441
J	CYS548
J	ASP550
K	ASP497
K	TYR499

site_id	CC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP L 11

Chain	Residue
K	MG31
K	PRO435
K	ASN436
K	THR437
K	GLY438
K	LYS439
K	SER440
K	ASP479
L	ASP489
L	THR490
L	ARG493

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04000

Chain	Residue	Details
A	GLY433
J	GLY433
K	GLY433
L	GLY433
B	GLY433
C	GLY433
D	GLY433
E	GLY433
F	GLY433
G	GLY433
H	GLY433
I	GLY433

site_id	SWS_FT_FI2
Number of Residues	24
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000255\|HAMAP-Rule:MF_04000, ECO:0000269\|PubMed:11005821

Chain	Residue	Details
A	LYS514
F	LYS514
G	LYS514
H	LYS514
I	LYS514
J	LYS514
K	LYS514
L	LYS514
B	LYS514
C	LYS514
D	LYS514
E	LYS514

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)