Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HU2

Structure of p97 N-D1 R86A mutant in complex with ATPgS

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AGS A 800

Chain	Residue
A	ASP205
A	LEU253
A	ASN348
A	ILE380
A	HIS384
A	GLY408
A	ALA409
A	MG801
A	HOH802
A	HOH803
A	HOH804
A	ILE206
B	ARG359
B	PHE360
A	GLY207
A	PRO247
A	GLY248
A	THR249
A	GLY250
A	LYS251
A	THR252

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	THR252
A	AGS800
A	HOH802
A	HOH803
A	HOH804

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AGS 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	ASN348
B	ILE380
B	HIS384
B	GLY408
B	ALA409
B	MG801
B	HOH802
B	HOH803
B	HOH804
C	ARG359
C	PHE360

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 801

Chain	Residue
B	THR252
B	AGS800
B	HOH802
B	HOH803
B	HOH804

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE AGS 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	ASN348
C	ILE380
C	HIS384
C	GLY408
C	ALA409
C	MG801
C	HOH802
C	HOH804
D	ARG359
D	PHE360

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 801

Chain	Residue
C	THR252
C	AGS800
C	HOH802
C	HOH803
C	HOH804

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE AGS D 800

Chain	Residue
D	ASP205
D	ILE206
D	GLY207
D	PRO247
D	GLY248
D	THR249
D	GLY250
D	LYS251
D	THR252
D	LEU253
D	ASN348
D	ILE380
D	HIS384
D	GLY408
D	ALA409
D	MG801
D	HOH803
D	HOH804
E	ARG359
E	PHE360

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 801

Chain	Residue
D	HOH803
D	HOH804
D	THR252
D	AGS800

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AGS E 800

Chain	Residue
E	ASP205
E	ILE206
E	GLY207
E	PRO247
E	GLY248
E	THR249
E	GLY250
E	LYS251
E	THR252
E	LEU253
E	ASN348
E	ILE380
E	HIS384
E	GLY408
E	ALA409
E	MG801
E	HOH802
E	HOH803
E	HOH804
F	ARG359
F	PHE360

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 801

Chain	Residue
E	THR252
E	AGS800
E	HOH802
E	HOH803
E	HOH804

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE AGS F 800

Chain	Residue
A	ARG359
A	PHE360
F	ASP205
F	ILE206
F	GLY207
F	PRO247
F	GLY248
F	THR249
F	GLY250
F	LYS251
F	THR252
F	LEU253
F	ASN348
F	ILE380
F	HIS384
F	GLY408
F	ALA409
F	MG801
F	HOH802
F	HOH804

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 801

Chain	Residue
F	THR252
F	AGS800
F	HOH802
F	HOH803
F	HOH804

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	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:20512113

Chain	Residue	Details
A	PRO247
D	PRO247
D	ASN348
D	HIS384
E	PRO247
E	ASN348
E	HIS384
F	PRO247
F	ASN348
F	HIS384
A	ASN348
A	HIS384
B	PRO247
B	ASN348
B	HIS384
C	PRO247
C	ASN348
C	HIS384

site_id	SWS_FT_FI2
Number of Residues	6
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

site_id	SWS_FT_FI3
Number of Residues	6
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

site_id	SWS_FT_FI4
Number of Residues	18
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER7
D	SER7
D	SER13
D	SER462
E	SER7
E	SER13
E	SER462
F	SER7
F	SER13
F	SER462
A	SER13
A	SER462
B	SER7
B	SER13
B	SER462
C	SER7
C	SER13
C	SER462

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
A	SER37
B	SER37
C	SER37
D	SER37
E	SER37
F	SER37

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269\|PubMed:22948820, ECO:0000269\|PubMed:23349634

Chain	Residue	Details
A	LYS315
B	LYS315
C	LYS315
D	LYS315
E	LYS315
F	LYS315

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18691976

Chain	Residue	Details
A	THR436
B	THR436
C	THR436
D	THR436
E	THR436
F	THR436

site_id	SWS_FT_FI8
Number of Residues	18
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS8
D	LYS8
D	LYS18
E	LYS8
E	LYS18
F	LYS8
F	LYS18
A	LYS18
B	LYS8
B	LYS18
C	LYS8
C	LYS18

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