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

5IFS

Quantitative interaction mapping reveals an extended ubiquitin regulatory domain in ASPL that disrupts functional p97 hexamers and induces cell death

Functional Information from GO Data
ChainGOidnamespacecontents
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ADP B 501
ChainResidue
BASP205
BHIS384
BGLY408
BALA409
BMG502
BHOH656
BHOH661
BGLY207
BGLY248
BTHR249
BGLY250
BLYS251
BTHR252
BLEU253
BILE380

site_idAC2
Number of Residues1
Detailsbinding site for residue MG B 502
ChainResidue
BADP501

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 B 503
ChainResidue
BARG359
BARG362
BHOH699

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO B 504
ChainResidue
BARG147
BLYS148

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO B 505
ChainResidue
BASN36
BLEU153
BVAL154
BARG155
BHOH660
BHOH723

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL B 506
ChainResidue
BTHR180
BILE182
BHOH685

site_idAC7
Number of Residues14
Detailsbinding site for residue ADP D 501
ChainResidue
DASP205
DGLY207
DGLY248
DTHR249
DGLY250
DLYS251
DTHR252
DLEU253
DILE380
DHIS384
DGLY408
DALA409
DMG502
DHOH629

site_idAC8
Number of Residues1
Detailsbinding site for residue MG D 502
ChainResidue
DADP501

site_idAC9
Number of Residues2
Detailsbinding site for residue EDO D 503
ChainResidue
DGLN398
DHOH616

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512113
ChainResidueDetails
BPRO247
BASN348
BHIS384
DPRO247
DASN348
DHIS384

site_idSWS_FT_FI2
Number of Residues2
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
DALA2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER3
DSER3

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER7
BSER13
BSER462
DSER7
DSER13
DSER462

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER37
DSER37

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634
ChainResidueDetails
BLYS315
DLYS315

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR436
DTHR436

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS8
BLYS18
DLYS8
DLYS18

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon