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3D2E

Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0005524molecular_functionATP binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 1001
ChainResidue
AGLY10
AGLU272
ALYS275
ASER279
AGLY342
AGLY343
ATHR344
AARG346
AILE347
BGLN33
AASN11
AASN12
AASN13
ALYS69
AGLY205
AHIS206
ASER207
ASER208

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP C 1001
ChainResidue
CGLY10
CASN11
CASN12
CASN13
CLYS69
CGLY205
CHIS206
CSER207
CSER208
CGLY234
CGLU272
CLYS275
CLYS276
CSER279
CGLY342
CGLY343
CTHR344
CARG346
CILE347
DGLN33

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 2002
ChainResidue
AARG162
APRO168
AASP485
ASER487

Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS
ChainResidueDetails
BILE9-SER16

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL
ChainResidueDetails
BILE197-LEU210
APHE201-MSE214

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. LvLvGGsTRIPkVqK
ChainResidueDetails
BLEU334-LYS348
AVAL338-GLN352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"9298649","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
BLYS71

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
DLYS71

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
ALYS69

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
CLYS69

239803

PDB entries from 2025-08-06

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