Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HD0

Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005737cellular_componentcytoplasm
D0032984biological_processprotein-containing complex disassembly
D0035265biological_processorgan growth
D0051117molecular_functionATPase binding
E0005737cellular_componentcytoplasm
E0032984biological_processprotein-containing complex disassembly
E0035265biological_processorgan growth
E0051117molecular_functionATPase binding
F0005737cellular_componentcytoplasm
F0032984biological_processprotein-containing complex disassembly
F0035265biological_processorgan growth
F0051117molecular_functionATPase binding
G0005737cellular_componentcytoplasm
G0032984biological_processprotein-containing complex disassembly
G0035265biological_processorgan growth
G0051117molecular_functionATPase binding
I0005737cellular_componentcytoplasm
I0032984biological_processprotein-containing complex disassembly
I0035265biological_processorgan growth
I0051117molecular_functionATPase binding
K0005737cellular_componentcytoplasm
K0032984biological_processprotein-containing complex disassembly
K0035265biological_processorgan growth
K0051117molecular_functionATPase binding
T0005524molecular_functionATP binding
T0016887molecular_functionATP hydrolysis activity
U0005524molecular_functionATP binding
U0016887molecular_functionATP hydrolysis activity
V0005524molecular_functionATP binding
V0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ADP B 501
ChainResidue
BILE206
CARG359
BGLY207
BTHR249
BGLY250
BLYS251
BTHR252
BLEU253
BHIS384
BALA409

site_idAC2
Number of Residues11
Detailsbinding site for residue ADP T 501
ChainResidue
TGLY207
TGLY248
TTHR249
TGLY250
TLYS251
TTHR252
TLEU253
THIS384
TALA409
UARG359
UPHE360

site_idAC3
Number of Residues8
Detailsbinding site for residue ADP U 501
ChainResidue
UGLY207
UGLY248
UTHR249
UGLY250
UHIS384
UALA409
UALA412
VARG359

site_idAC4
Number of Residues10
Detailsbinding site for residue ADP V 501
ChainResidue
AARG359
VASP205
VILE206
VGLY207
VTHR249
VGLY250
VTHR252
VLEU253
VHIS384
VALA409

site_idAC5
Number of Residues9
Detailsbinding site for residue ADP A 501
ChainResidue
AGLY207
AGLY248
ATHR249
AGLY250
ALYS251
ATHR252
AILE380
AHIS384
BARG359

site_idAC6
Number of Residues10
Detailsbinding site for residue ADP C 501
ChainResidue
CASP205
CILE206
CGLY207
CTHR249
CGLY250
CTHR252
CLEU253
CHIS384
CALA409
TARG359

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
BVAL341-ARG359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512113
ChainResidueDetails
BPRO247
VPRO247
VASN348
VHIS384
APRO247
AASN348
AHIS384
CPRO247
CASN348
CHIS384
BASN348
BHIS384
TPRO247
TASN348
THIS384
UPRO247
UASN348
UHIS384

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_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
ChainResidueDetails
BALA2
TALA2
UALA2
VALA2
AALA2
CALA2

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER3
TSER3
USER3
VSER3
ASER3
CSER3

site_idSWS_FT_FI4
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER7
VSER7
VSER13
VSER462
ASER7
ASER13
ASER462
CSER7
CSER13
CSER462
BSER13
BSER462
TSER7
TSER13
TSER462
USER7
USER13
USER462

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER37
TSER37
USER37
VSER37
ASER37
CSER37

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634
ChainResidueDetails
BLYS315
TLYS315
ULYS315
VLYS315
ALYS315
CLYS315

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR436
TTHR436
UTHR436
VTHR436
ATHR436
CTHR436

site_idSWS_FT_FI8
Number of Residues18
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS8
VLYS8
VLYS18
ALYS8
ALYS18
CLYS8
CLYS18
BLYS18
TLYS8
TLYS18
ULYS8
ULYS18

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon