Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5DYI

Structure of p97 N-D1 wild-type in complex with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0016887	molecular_function	ATP hydrolysis activity
C	0005524	molecular_function	ATP binding
C	0016887	molecular_function	ATP hydrolysis activity
D	0005524	molecular_function	ATP binding
D	0016887	molecular_function	ATP hydrolysis activity
E	0005524	molecular_function	ATP binding
E	0016887	molecular_function	ATP hydrolysis activity
F	0005524	molecular_function	ATP binding
F	0016887	molecular_function	ATP hydrolysis activity
G	0005524	molecular_function	ATP binding
G	0016887	molecular_function	ATP hydrolysis activity
H	0005524	molecular_function	ATP binding
H	0016887	molecular_function	ATP hydrolysis activity
I	0005524	molecular_function	ATP binding
I	0016887	molecular_function	ATP hydrolysis activity
J	0005524	molecular_function	ATP binding
J	0016887	molecular_function	ATP hydrolysis activity
K	0005524	molecular_function	ATP binding
K	0016887	molecular_function	ATP hydrolysis activity
L	0005524	molecular_function	ATP binding
L	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ADP A 800

Chain	Residue
A	ASP205
A	ASP304
A	ILE380
A	HIS384
A	GLY408
A	ALA409
B	ARG359
A	ILE206
A	GLY207
A	GLY248
A	THR249
A	GLY250
A	LYS251
A	THR252
A	LEU253

site_id	AC2
Number of Residues	15
Details	binding site for residue ADP B 800

Chain	Residue
B	ASP205
B	GLY207
B	PRO247
B	GLY248
B	THR249
B	GLY250
B	LYS251
B	THR252
B	LEU253
B	ASP304
B	ILE380
B	HIS384
B	GLY408
B	ALA409
C	ARG359

site_id	AC3
Number of Residues	14
Details	binding site for residue ADP C 800

Chain	Residue
C	ASP205
C	GLY207
C	GLY248
C	THR249
C	GLY250
C	LYS251
C	THR252
C	LEU253
C	ASP304
C	ILE380
C	HIS384
C	GLY408
C	ALA409
D	ARG359

site_id	AC4
Number of Residues	14
Details	binding site for residue ADP D 800

Chain	Residue
D	ASP205
D	GLY207
D	GLY248
D	THR249
D	GLY250
D	LYS251
D	THR252
D	LEU253
D	ASP304
D	ILE380
D	HIS384
D	GLY408
D	ALA409
E	ARG359

site_id	AC5
Number of Residues	14
Details	binding site for residue ADP E 800

Chain	Residue
E	ASP205
E	GLY207
E	GLY248
E	THR249
E	GLY250
E	LYS251
E	THR252
E	LEU253
E	ASP304
E	ILE380
E	HIS384
E	GLY408
E	ALA409
F	ARG359

site_id	AC6
Number of Residues	14
Details	binding site for residue ADP F 800

Chain	Residue
A	ARG359
F	ASP205
F	GLY207
F	GLY248
F	THR249
F	GLY250
F	LYS251
F	THR252
F	LEU253
F	ASP304
F	ILE380
F	HIS384
F	GLY408
F	ALA409

site_id	AC7
Number of Residues	14
Details	binding site for residue ADP G 800

Chain	Residue
H	ARG359
G	ASP205
G	GLY207
G	GLY248
G	THR249
G	GLY250
G	LYS251
G	THR252
G	LEU253
G	ASP304
G	ILE380
G	HIS384
G	GLY408
G	ALA409

site_id	AC8
Number of Residues	14
Details	binding site for residue ADP H 800

Chain	Residue
H	ASP205
H	GLY207
H	PRO247
H	GLY248
H	THR249
H	GLY250
H	LYS251
H	THR252
H	LEU253
H	ILE380
H	HIS384
H	GLY408
H	ALA409
I	ARG359

site_id	AC9
Number of Residues	14
Details	binding site for residue ADP I 800

Chain	Residue
I	ASP205
I	GLY207
I	GLY248
I	THR249
I	GLY250
I	LYS251
I	THR252
I	LEU253
I	ASP304
I	ILE380
I	HIS384
I	GLY408
I	ALA409
J	ARG359

site_id	AD1
Number of Residues	15
Details	binding site for residue ADP J 800

Chain	Residue
J	ASP205
J	GLY207
J	PRO247
J	GLY248
J	THR249
J	GLY250
J	LYS251
J	THR252
J	LEU253
J	ASP304
J	ILE380
J	HIS384
J	GLY408
J	ALA409
K	ARG359

site_id	AD2
Number of Residues	14
Details	binding site for residue ADP K 800

Chain	Residue
K	ASP205
K	GLY207
K	GLY248
K	THR249
K	GLY250
K	LYS251
K	THR252
K	LEU253
K	ASP304
K	ILE380
K	HIS384
K	GLY408
K	ALA409
L	ARG359

site_id	AD3
Number of Residues	14
Details	binding site for residue ADP L 800

Chain	Residue
G	ARG359
L	ASP205
L	GLY207
L	GLY248
L	THR249
L	GLY250
L	LYS251
L	THR252
L	LEU253
L	ASP304
L	ILE380
L	HIS384
L	GLY408
L	ALA409

Functional Information from PROSITE/UniProt

site_id	PS00674
Number of Residues	19
Details	AAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R

Chain	Residue	Details
A	VAL341-ARG359

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:20512113

Chain	Residue	Details
E	PRO247
E	ASN348
E	HIS384
F	PRO247
F	ASN348
F	HIS384
G	PRO247
G	ASN348
G	HIS384
H	PRO247
H	ASN348
H	HIS384
I	PRO247
I	ASN348
I	HIS384
J	PRO247
J	ASN348
J	HIS384
K	PRO247
K	ASN348
K	HIS384
L	PRO247
L	ASN348
L	HIS384
A	PRO247
A	ASN348
A	HIS384
B	PRO247
B	ASN348
B	HIS384
C	PRO247
C	ASN348
C	HIS384
D	PRO247
D	ASN348
D	HIS384

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.9, ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2
E	ALA2
F	ALA2
G	ALA2
H	ALA2
I	ALA2
J	ALA2
K	ALA2
L	ALA2

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER3
B	SER3
C	SER3
D	SER3
E	SER3
F	SER3
G	SER3
H	SER3
I	SER3
J	SER3
K	SER3
L	SER3

site_id	SWS_FT_FI4
Number of Residues	36
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
E	SER7
E	SER13
E	SER462
F	SER7
F	SER13
F	SER462
G	SER7
G	SER13
G	SER462
H	SER7
H	SER13
H	SER462
I	SER7
I	SER13
I	SER462
J	SER7
J	SER13
J	SER462
K	SER7
K	SER13
K	SER462
L	SER7
L	SER13
L	SER462
B	SER7
B	SER13
B	SER462
C	SER7
C	SER13
C	SER462
D	SER7
D	SER13
D	SER462
A	SER7
A	SER13
A	SER462

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
A	SER37
B	SER37
C	SER37
D	SER37
E	SER37
F	SER37
G	SER37
H	SER37
I	SER37
J	SER37
K	SER37
L	SER37

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269\|PubMed:22948820, ECO:0000269\|PubMed:23349634

Chain	Residue	Details
D	LYS315
E	LYS315
F	LYS315
G	LYS315
A	LYS315
B	LYS315
C	LYS315
H	LYS315
I	LYS315
J	LYS315
K	LYS315
L	LYS315

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18691976

Chain	Residue	Details
B	THR436
C	THR436
D	THR436
E	THR436
F	THR436
G	THR436
H	THR436
I	THR436
J	THR436
K	THR436
L	THR436
A	THR436

site_id	SWS_FT_FI8
Number of Residues	36
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
E	LYS8
E	LYS18
F	LYS8
F	LYS18
G	LYS8
G	LYS18
H	LYS8
H	LYS18
I	LYS8
I	LYS18
J	LYS8
J	LYS18
K	LYS8
K	LYS18
L	LYS8
L	LYS18
A	LYS8
A	LYS18
B	LYS8
B	LYS18
C	LYS8
C	LYS18
D	LYS8
D	LYS18

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