Structure of PDB 2qxl Chain A

Receptor sequence
>2qxlA (length=617) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGET
GKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGA
EVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEE
QRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFV
DIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKTK
YKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLS
REELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQ
SISEAFGKPLSTTLNQDEAIAKGAAFICAIHSRPFKFEDIHPYSVSYSWD
KQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPE
QIANWEITDSVPVKLKLRCDPSGLHTIEEAYTIEDKTVKKDDLTIVAHTF
GLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYA
PFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRG
RYLAKEEEKKQAIRSKQ
3D structure
PDB2qxl Insights into hsp70 chaperone activity from a crystal structure of the yeast hsp110 Sse1.
ChainA
Resolution2.41 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D8 K69 D174 D203
Catalytic site (residue number reindexed from 1) D6 K67 D172 D201
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ATP A G10 N11 N12 N13 K69 G205 H206 S207 E272 K275 K276 S279 G342 G343 T344 R346 G8 N9 N10 N11 K67 G203 H204 S205 E270 K273 K274 S277 G340 G341 T342 R344
Gene Ontology
Molecular Function
GO:0000774 adenyl-nucleotide exchange factor activity
GO:0005515 protein binding
GO:0005516 calmodulin binding
GO:0005524 ATP binding
GO:0042277 peptide binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0006914 autophagy
GO:0010499 proteasomal ubiquitin-independent protein catabolic process
GO:0042026 protein refolding
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2qxl, PDBe:2qxl, PDBj:2qxl
PDBsum2qxl
PubMed17923091
UniProtP32589|HSP7F_YEAST Heat shock protein homolog SSE1 (Gene Name=SSE1)

[Back to BioLiP]