General Information

Database accession: MF7000762

Name: Catechol 1,2-dioxygenase with Hg (Acinetobacter sp. ADP1)

PDB ID: 1dlq PDBe

Experimental method: X-ray (2.30 Å)

Assembly: Homodimer

Source organism: Acinetobacter baylyi

Primary publication of the structure:

Vetting MW, Ohlendorf DH
The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
(2000) Structure 8: 429-40

PMID: 10801478 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:

catechol 1,2-dioxygenase activity catechol 1,2-dioxygenase activity GeneOntology

ferric iron binding ferric iron binding GeneOntology

Biological process:

beta-ketoadipate pathway beta-ketoadipate pathway GeneOntology

catechol-containing compound catabolic process catechol-containing compound catabolic process GeneOntology

Cellular component: not assigned

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 2 distinct polypeptide molecules

Chains: A, B

Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.

Number of unique protein segments: 1


Chain A

Name: Catechol 1,2-dioxygenase

Source organism: Acinetobacter baylyi

Length: 311 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV

UniProtKB AC: P07773 (positions: 3-311) UniProt

Coverage: 99%

Chain B

Name: Catechol 1,2-dioxygenase

Source organism: Acinetobacter baylyi

Length: 311 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV

UniProtKB AC: P07773 (positions: 3-311) UniProt

Coverage: 99%

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: Dioxygenase

Evidence level: Indirect evidence

Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.

Complex Evidence:

A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478).

Chain A:

N/A

Chain B:

N/A

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).

There are 12 related structures in the MFIB database:






The molecule viewer shows our modified stucture.

Download the CIF file (.cif)

Download this entry's XML file (.xml)

Download this entry's JSON file (.json)