Structure of PDB 1w7a Chain A

Receptor sequence
>1w7aA (length=791) Species: 562 (Escherichia coli) [Search protein sequence]
SAIENFDAHTPMMQQYLRLKAQHPEILLFYRMGDFYELFYDDAKRASQLL
DISLTKRGASAGEPIPMAGIPYHAVENYLAKLVNQGESVAICEQIGDPAT
SKGPVERKVVRIVTPGTISDEALLQERQDNLLAAIWQDSKGFGYATLDIS
SGRFRLSEPADRETMAAELQRTNPAELLYAEDFAEMSLIEGRRGLRRRPL
WEFEIDTARQQLNLQFGTRDLVGFGVENAPRGLCAAGCLLQYAKDTQRTT
LPHIRSITMEREQDSIIMDAATRRNLEITQNLAGGAENTLASVLDCTVTP
MGSRMLKRWLHMPVRDTRVLLERQQTIGALQDFTAGLQPVLRQVGDLERI
LARLALRTARPRDLARMRHAFQQLPELRAQLETVDSAPVQALREKMGEFA
ELRDLLERAIIDTPPVLVRDGGVIASGYNEELDEWRALADGATDYLERLE
VRERERTGLDTLKVGFNAVHGYYIQISRGQSHLAPINYMRRQTLKNAERY
IIPELKEYEDKVLTSKGKALALEKQLYEELFDLLLPHLEALQQSASALAE
LDVLVNLAERAYTLNYTCPTFIDKPGIRITEGRHPVVEQVLNEPFIANPL
NLSPQRRMLIITGPNMGGKSTYMRQTALIALMAYIGSYVPAQKVEIGPID
RIFTRVGASTFMVEMTETANILHNATEYSLVLMDEIGRGTSTYDGLSLAW
ACAENLANKIKALTLFATHYFELTQLPEKMEGVANVHLDALEHGDTIAFM
HSVQDGAASKSYGLAVAALAGVPKEVIKRARQKLRELESIS
3D structure
PDB1w7a ATP Increases the Affinity between Muts ATPase Domains: Implications for ATP Hydrolysis and Conformational Changes
ChainA
Resolution2.27 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003684 damaged DNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008301 DNA binding, bending
GO:0016887 ATP hydrolysis activity
GO:0030983 mismatched DNA binding
GO:0032136 adenine/cytosine mispair binding
GO:0042802 identical protein binding
GO:0043531 ADP binding
GO:0140664 ATP-dependent DNA damage sensor activity
Biological Process
GO:0000018 regulation of DNA recombination
GO:0006281 DNA repair
GO:0006298 mismatch repair
GO:0006974 DNA damage response
Cellular Component
GO:0005829 cytosol
GO:0032300 mismatch repair complex
GO:1990710 MutS complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1w7a, PDBe:1w7a, PDBj:1w7a
PDBsum1w7a
PubMed15297450
UniProtP23909|MUTS_ECOLI DNA mismatch repair protein MutS (Gene Name=mutS)

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