General Information

Database accession: MF2120007 Original MFIB entry

Name: UmuD' protein filament

PDB ID: 1ay9 PDBe

Experimental method: X-ray (3.00 Å)

Assembly: Homodimer

Source organism: Escherichia coli

Primary publication of the structure:

Peat TS, Frank EG, McDonald JP, Levine AS, Woodgate R, Hendrickson WA
The UmuD' protein filament and its potential role in damage induced mutagenesis.
(1996) Structure 4: 1401-12

PMID: 8994967 PubMed

Abstract:

Not available.

Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

ATP-dependent activity, acting on DNA ATP-dependent activity, acting on DNA GeneOntology

DNA-directed DNA polymerase activity DNA-directed DNA polymerase activity GeneOntology

identical protein binding identical protein binding GeneOntology

nucleic acid binding nucleic acid binding GeneOntology

serine-type peptidase activity serine-type peptidase activity GeneOntology

single-stranded DNA binding single-stranded DNA binding GeneOntology

Biological process:

DNA damage response DNA damage response GeneOntology

DNA repair DNA repair GeneOntology

proteolysis proteolysis GeneOntology

regulation of DNA-templated transcription regulation of DNA-templated transcription GeneOntology

SOS response SOS response GeneOntology

translesion synthesis translesion synthesis GeneOntology

Cellular component:

DNA polymerase V complex DNA polymerase V complex GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 2 distinct polypeptide molecules

Chains: A, B-2

Notes: According to the most probable oligomerization state stored in PDBe B,A-2 chains were not considered.

Number of unique protein segments: 1

Chain A

Name: Protein UmuD

Source organism: Escherichia coli

Length: 139 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR

UniProtKB AC: P0AG11 (positions: 32-139) UniProt

Coverage: 77%

Chain B-2

Name: Protein UmuD

Source organism: Escherichia coli

Length: 139 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR

UniProtKB AC: P0AG11 (positions: 32-139) UniProt

Coverage: 77%

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Representative domain in related structures: -

Evidence level: Direct evidence

Evidence coverage: The full structure participates in mutual synergistic folding.

Complex Evidence:

None

Chain A:

The region(s) described in DP00626 covers 100% of the sequence present in the structure

Chain B-2:

The region(s) described in DP00626 covers 100% of the sequence present in the structure

Surface and contacts features:

Related Structure(s) Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap).

No related structure was found in the MFIB database.

The molecule viewer shows our modified stucture.

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