Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6MCK

p97 D1D2 with CB5083 bound

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	12
Details	binding site for residue JDP A 900

Chain	Residue
A	ASP478
A	GLY684
A	ALA685
A	THR688
A	ILE479
A	LEU482
A	GLY523
A	LEU526
A	ILE656
A	ALA659
A	ASN660
A	ARG662

site_id	AC2
Number of Residues	14
Details	binding site for residue JDP B 900

Chain	Residue
B	VAL474
B	ASP478
B	ILE479
B	LEU482
B	CYS522
B	GLY523
B	LEU526
B	ILE656
B	ALA659
B	ASN660
B	ARG662
B	GLY684
B	ALA685
B	THR688

site_id	AC3
Number of Residues	12
Details	binding site for residue JDP C 900

Chain	Residue
C	VAL474
C	ASP478
C	ILE479
C	LEU482
C	GLY523
C	LEU526
C	ILE656
C	ALA659
C	ARG662
C	GLY684
C	ALA685
C	THR688

site_id	AC4
Number of Residues	14
Details	binding site for residue JDP D 900

Chain	Residue
D	ASP478
D	ILE479
D	LEU482
D	CYS522
D	GLY523
D	LEU526
D	SER652
D	ILE656
D	ALA659
D	ASN660
D	ARG662
D	GLY684
D	ALA685
D	THR688

site_id	AC5
Number of Residues	14
Details	binding site for residue JDP E 900

Chain	Residue
E	ASP478
E	ILE479
E	LEU482
E	CYS522
E	GLY523
E	LEU526
E	ALA655
E	ILE656
E	ALA659
E	ASN660
E	ARG662
E	GLY684
E	ALA685
E	THR688

site_id	AC6
Number of Residues	11
Details	binding site for residue JDP F 900

Chain	Residue
F	ASP478
F	ILE479
F	LEU482
F	GLY523
F	LEU526
F	ILE656
F	ALA659
F	ARG662
F	GLY684
F	ALA685
F	THR688

site_id	AC7
Number of Residues	11
Details	binding site for residue JDP G 900

Chain	Residue
G	ASP478
G	ILE479
G	GLY523
G	LEU526
G	ILE656
G	ALA659
G	ASN660
G	ARG662
G	GLY684
G	ALA685
G	THR688

site_id	AC8
Number of Residues	15
Details	binding site for residue JDP H 900

Chain	Residue
H	ARG662
H	GLY684
H	ALA685
H	THR688
H	VAL474
H	ASP478
H	ILE479
H	LEU482
H	CYS522
H	GLY523
H	LEU526
H	LEU527
H	ILE656
H	ALA659
H	ASN660

site_id	AC9
Number of Residues	13
Details	binding site for residue JDP I 900

Chain	Residue
I	ASP478
I	ILE479
I	LEU482
I	CYS522
I	GLY523
I	LEU526
I	ILE656
I	ALA659
I	ASN660
I	ARG662
I	GLY684
I	ALA685
I	THR688

site_id	AD1
Number of Residues	13
Details	binding site for residue JDP J 900

Chain	Residue
J	ASP478
J	ILE479
J	LEU482
J	GLY523
J	LEU526
J	SER652
J	ILE656
J	ALA659
J	ASN660
J	ARG662
J	GLY684
J	ALA685
J	THR688

site_id	AD2
Number of Residues	13
Details	binding site for residue JDP K 900

Chain	Residue
K	ASP478
K	ILE479
K	LEU482
K	CYS522
K	GLY523
K	LEU526
K	ILE656
K	ALA659
K	ASN660
K	ARG662
K	GLY684
K	ALA685
K	THR688

site_id	AD3
Number of Residues	11
Details	binding site for residue JDP L 900

Chain	Residue
L	ASP478
L	ILE479
L	GLY523
L	LEU526
L	ILE656
L	ALA659
L	ASN660
L	ARG662
L	GLY684
L	ALA685
L	THR688

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
A	VAL617-ARG635

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
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
G	PRO247
A	ASN348
G	ASN348
G	HIS384
H	PRO247
H	ASN348
H	HIS384
I	PRO247
I	ASN348
I	HIS384
J	PRO247
J	ASN348
A	HIS384
J	HIS384
K	PRO247
K	ASN348
K	HIS384
L	PRO247
L	ASN348
L	HIS384
B	PRO247
B	ASN348
B	HIS384
C	PRO247
C	ASN348
C	HIS384

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q01853

Chain	Residue	Details
A	GLY521
J	GLY521
K	GLY521
L	GLY521
B	GLY521
C	GLY521
D	GLY521
E	GLY521
F	GLY521
G	GLY521
H	GLY521
I	GLY521

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269\|PubMed:22948820, ECO:0000269\|PubMed:23349634

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

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18691976

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

site_id	SWS_FT_FI5
Number of Residues	24
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER462
E	SER702
F	SER462
F	SER702
G	SER462
G	SER702
H	SER462
H	SER702
I	SER462
I	SER702
J	SER462
A	SER702
J	SER702
K	SER462
K	SER702
L	SER462
L	SER702
B	SER462
B	SER702
C	SER462
C	SER702
D	SER462
D	SER702
E	SER462

site_id	SWS_FT_FI6
Number of Residues	36
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q01853

Chain	Residue	Details
A	LYS502
D	LYS502
D	LYS505
D	LYS754
E	LYS502
E	LYS505
E	LYS754
F	LYS502
F	LYS505
F	LYS754
G	LYS502
A	LYS505
G	LYS505
G	LYS754
H	LYS502
H	LYS505
H	LYS754
I	LYS502
I	LYS505
I	LYS754
J	LYS502
J	LYS505
A	LYS754
J	LYS754
K	LYS502
K	LYS505
K	LYS754
L	LYS502
L	LYS505
L	LYS754
B	LYS502
B	LYS505
B	LYS754
C	LYS502
C	LYS505
C	LYS754

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q01853

Chain	Residue	Details
A	LYS668
J	LYS668
K	LYS668
L	LYS668
B	LYS668
C	LYS668
D	LYS668
E	LYS668
F	LYS668
G	LYS668
H	LYS668
I	LYS668

site_id	SWS_FT_FI8
Number of Residues	24
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
A	SER770
E	SER775
F	SER770
F	SER775
G	SER770
G	SER775
H	SER770
H	SER775
I	SER770
I	SER775
J	SER770
A	SER775
J	SER775
K	SER770
K	SER775
L	SER770
L	SER775
B	SER770
B	SER775
C	SER770
C	SER775
D	SER770
D	SER775
E	SER770

site_id	SWS_FT_FI9
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976

Chain	Residue	Details
A	SER787
J	SER787
K	SER787
L	SER787
B	SER787
C	SER787
D	SER787
E	SER787
F	SER787
G	SER787
H	SER787
I	SER787

site_id	SWS_FT_FI10
Number of Residues	12
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q01853

Chain	Residue	Details
A	TYR805
J	TYR805
K	TYR805
L	TYR805
B	TYR805
C	TYR805
D	TYR805
E	TYR805
F	TYR805
G	TYR805
H	TYR805
I	TYR805

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