Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KOD

Structure of p97 N-D1 R155H mutant 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	17
Details	BINDING SITE FOR RESIDUE ADP A 800

Chain	Residue
A	ASP205
A	LEU253
A	ILE380
A	HIS384
A	GLY408
A	ALA409
A	HOH903
A	HOH908
E	ARG359
A	ILE206
A	GLY207
A	PRO247
A	GLY248
A	THR249
A	GLY250
A	LYS251
A	THR252

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP B 800

Chain	Residue
B	ASP205
B	ILE206
B	GLY207
B	PRO247
B	GLY248
B	THR249
B	GLY250
B	LYS251
B	THR252
B	LEU253
B	ILE380
B	HIS384
B	GLY408
B	ALA409
B	HOH903
F	ARG359
F	PHE360

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP C 800

Chain	Residue
C	ASP205
C	ILE206
C	GLY207
C	PRO247
C	GLY248
C	THR249
C	GLY250
C	LYS251
C	THR252
C	LEU253
C	ILE380
C	HIS384
C	GLY408
C	ALA409
C	HOH903
D	ARG359
D	HOH906

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP D 800

Chain	Residue
B	ARG359
B	PHE360
D	ASP205
D	ILE206
D	GLY207
D	PRO247
D	GLY248
D	THR249
D	GLY250
D	LYS251
D	THR252
D	LEU253
D	ILE380
D	HIS384
D	GLY408
D	ALA409

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP E 800

Chain	Residue
C	ARG359
C	PHE360
E	ASP205
E	ILE206
E	GLY207
E	PRO247
E	GLY248
E	THR249
E	GLY250
E	LYS251
E	THR252
E	LEU253
E	ILE380
E	HIS384
E	GLY408
E	ALA409
E	HOH911

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP F 800

Chain	Residue
A	ARG359
F	ASP205
F	ILE206
F	GLY207
F	PRO247
F	GLY248
F	THR249
F	GLY250
F	LYS251
F	THR252
F	LEU253
F	ILE380
F	HIS384
F	GLY408
F	ALA409

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP G 800

Chain	Residue
G	ASP205
G	ILE206
G	GLY207
G	PRO247
G	GLY248
G	THR249
G	GLY250
G	LYS251
G	THR252
G	LEU253
G	ILE380
G	HIS384
G	GLY408
G	ALA409
G	HOH908
K	ARG359

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP H 800

Chain	Residue
H	ASP205
H	ILE206
H	GLY207
H	PRO247
H	GLY248
H	THR249
H	GLY250
H	LYS251
H	THR252
H	LEU253
H	ILE380
H	HIS384
H	GLY408
H	ALA409
H	HOH909
L	ARG359
L	PHE360

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP I 800

Chain	Residue
I	ASP205
I	ILE206
I	GLY207
I	PRO247
I	GLY248
I	THR249
I	GLY250
I	LYS251
I	THR252
I	LEU253
I	ILE380
I	HIS384
I	GLY408
I	ALA409
I	HOH906
J	ARG359
J	PHE360

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP J 800

Chain	Residue
H	ARG359
H	PHE360
J	ASP205
J	ILE206
J	GLY207
J	PRO247
J	GLY248
J	THR249
J	GLY250
J	LYS251
J	THR252
J	LEU253
J	ILE380
J	HIS384
J	GLY408
J	ALA409

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP K 800

Chain	Residue
I	ARG359
K	ASP205
K	ILE206
K	GLY207
K	PRO247
K	GLY248
K	THR249
K	GLY250
K	LYS251
K	THR252
K	LEU253
K	ILE380
K	HIS384
K	GLY408
K	ALA409
K	HOH904

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP L 800

Chain	Residue
G	ARG359
L	ASP205
L	ILE206
L	GLY207
L	PRO247
L	GLY248
L	THR249
L	GLY250
L	LYS251
L	THR252
L	LEU253
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	96
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20512113","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine; by VCPKMT","evidences":[{"source":"PubMed","id":"22948820","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23349634","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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