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2QXL

Crystal Structure Analysis of Sse1, a yeast Hsp110

Functional Information from GO Data
ChainGOidnamespacecontents
A0000774molecular_functionadenyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0006914biological_processautophagy
A0010499biological_processproteasomal ubiquitin-independent protein catabolic process
A0042026biological_processprotein refolding
A0042277molecular_functionpeptide binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0140662molecular_functionATP-dependent protein folding chaperone
B0000774molecular_functionadenyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006914biological_processautophagy
B0010499biological_processproteasomal ubiquitin-independent protein catabolic process
B0042026biological_processprotein refolding
B0042277molecular_functionpeptide binding
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1003
ChainResidue
BATP1001
BHOH1165
BHOH1215
BHOH1218
BHOH1220

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1004
ChainResidue
AATP1002
AHOH1067
AHOH1119

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 1005
ChainResidue
AASN13
AATP1002
AHOH1089
AASP8

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 1006
ChainResidue
BASP8
BASN13
BATP1001
BHOH1037

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE ATP B 1001
ChainResidue
BGLY10
BASN11
BASN12
BASN13
BLYS69
BGLY205
BHIS206
BSER207
BSER208
BGLY234
BGLU272
BLYS275
BLYS276
BSER279
BGLY342
BGLY343
BTHR344
BARG346
BILE347
BMG1003
BK1006
BHOH1018
BHOH1028
BHOH1046
BHOH1056
BHOH1158
BHOH1165
BHOH1215
BHOH1218
BHOH1220
BHOH1224

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP A 1002
ChainResidue
AGLY10
AASN11
AASN12
AASN13
ALYS69
AGLY205
AHIS206
ASER207
ASER208
AGLY234
AGLU272
ALYS275
ALYS276
ASER279
AGLY342
AGLY343
ATHR344
AARG346
AMG1004
AK1005
AHOH1006
AHOH1022
AHOH1047
AHOH1054
AHOH1067
AHOH1079
AHOH1119

Functional Information from PROSITE/UniProt
site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. FVDIGHSSytcSIM
ChainResidueDetails
APHE201-MET214

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. VeIiGGtTRIPtLkQ
ChainResidueDetails
AVAL338-GLN352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:9298649
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ATHR242
BTHR242

site_idSWS_FT_FI3
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS195
BLYS195

220472

PDB entries from 2024-05-29

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