Structure of PDB 1ulj Chain A

Receptor sequence

>1uljA (length=425) Species: 101510 (Rhodococcus jostii RHA1)

WADADIAELVDERTGRLDPRIYTDEALYEQELERIFGRSWLLMGHETQIP
KAGDFMTNYMGEDPVMVVRQKNGEIRVFLNQCRHRGMRICRADGGNAKSF
TCSYHGWAYDTGGNLVSVPFEEQAFPGLRKEDWGPLQARVETYKGLIFAN
WDADAPDLDTYLGEAKFYMDHMLDRTEAGTEAIPGIQKWVIPCNWKFAAE
QFCSDMYHAGTTSHLSGILAGLPPTEGIQYRATWGGHGSGFYIGDPNLLL
AIMGPKVTEYWTQGPAAEKASERLGSTERGQQLMAQHMTIFPTCSFLPGI
NTIRAWHPRGPNEIEVWAFTVVDADAPEEMKEEYRQQTLRTFSAGGVFEQ
DDGENWVEIQQVLRGHKARSRPFNAEMGLGQTDSDNPDYPGTISYVYSEE
AARGLYTQWVRMMTSPDWAALDATR

3D structure

• PDB: 1ulj Crystal Structure of the Terminal Oxygenase Component of Biphenyl Dioxygenase Derived from Rhodococcus sp. Strain RHA1
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H121 D221 H224 H230 D378
• Catalytic site (residue number reindexed from 1): H105 D205 H208 H214 D352
• Enzyme Commision number: 1.14.12.18: biphenyl 2,3-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	FE2	A	Q217 H224 H230 D378	Q201 H208 H214 D352
BS02	FES	A	C98 H100 R101 M103 C118 Y120 H121 W123	C82 H84 R85 M87 C102 Y104 H105 W107
BS03	BNL	A	Q217 F218 D221 M222 H224 A225 H230 I278 H313 L323 F368	Q201 F202 D205 M206 H208 A209 H214 I252 H287 L297 F342

Gene Ontology

Molecular Function

• GO:0005506 iron ion binding
• GO:0005515 protein binding
• GO:0018687 biphenyl 2,3-dioxygenase activity
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity
• GO:0051537 2 iron, 2 sulfur cluster binding

Biological Process

• GO:0009056 catabolic process
• GO:0044237 cellular metabolic process

External links

• PDB: RCSB:1ulj, PDBe:1ulj, PDBj:1ulj
• PDBsum: 1ulj
• PubMed: 15342255
• UniProt: Q53122|BPHA1_RHOJR Biphenyl 2,3-dioxygenase subunit alpha (Gene Name=bphA1)