Structure of PDB 2hj4 Chain B

Receptor sequence
>2hj4B (length=358) Species: 511 (Alcaligenes faecalis) [Search protein sequence]
REVLTGGHSVSAPQENRIYVMDSVFMHLTESRVHVYDYTNGKFLGMVPTA
FNGHVQVSNDGKKIYTMTTYHERITRGKRSDVVEVWDADKLTFEKEISLP
PKRVQGLNYDGLFRQTTDGKFIVLQNASPATSIGIVDVAKGDYVEDVTAA
AGCWSVIPQPNRPRSFMTICGDGGLLTINLGEDGKVASQSRSKQMFSVKD
DPIFIAPALDKDKAHFVSYYGNVYSADFSGDEVKVDGPWSLLNDEDKAKN
WVPGGYNLVGLHRASGRMYVFMHPDGKEGTHKFPAAEIWVMDTKTKQRVA
RIPGRDALSMTIDQQRNLMLTLDGGNVNVYDISQPEPKLLRTIEGAAEAS
LQVQFHPV
3D structure
PDB2hj4 Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M98
Catalytic site (residue number reindexed from 1) M26
Enzyme Commision number 1.4.9.2: aralkylamine dehydrogenase (azurin).
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 PNZ B F123 N124 G178 F51 N52 G106 PDBbind-CN: -logKd/Ki=5.37,Kd=4.29uM
BS02 PNZ B Y328 L380 A421 L423 Y256 L308 A349 L351 PDBbind-CN: -logKd/Ki=5.37,Kd=4.29uM
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0030058 aliphatic amine dehydrogenase activity
GO:0030059 aralkylamine dehydrogenase (azurin) activity
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:2hj4, PDBe:2hj4, PDBj:2hj4
PDBsum2hj4
PubMed17636875
UniProtP84888|AAUB_ALCFA Aralkylamine dehydrogenase heavy chain (Gene Name=aauB)

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