Structure of PDB 1dlt Chain B

Receptor sequence

>1dltB (length=309) Species: 62977 (Acinetobacter baylyi ADP1)

VKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITS
DEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATP
RTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAK
VEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGC
PPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDD
FAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQ
VVDRPRLAV

3D structure

• PDB: 1dlt The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y164 Y200 R221 H224 H226
• Catalytic site (residue number reindexed from 1): Y162 Y198 R219 H222 H224
• Enzyme Commision number: 1.13.11.1: catechol 1,2-dioxygenase.

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	FE	B	Y164 H224 H226	Y162 H222 H224
BS02	CAQ	B	P108 Y164 Y200 R221 H224 H226	P106 Y162 Y198 R219 H222 H224

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005506 iron ion binding
• GO:0008199 ferric iron binding
• GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
• GO:0018576 catechol 1,2-dioxygenase activity
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

Biological Process

• GO:0009056 catabolic process
• GO:0009712 catechol-containing compound metabolic process
• GO:0019614 catechol-containing compound catabolic process
• GO:0042952 beta-ketoadipate pathway

Cellular Component

• GO:0005575 cellular_component

External links

• PDB: RCSB:1dlt, PDBe:1dlt, PDBj:1dlt
• PDBsum: 1dlt
• PubMed: 10801478
• UniProt: P07773|CATA_ACIAD Catechol 1,2-dioxygenase (Gene Name=catA)