Structure of PDB 4zm4 Chain E

Receptor sequence
>4zm4E (length=425) Species: 68249 (Streptomyces pactum) [Search protein sequence]
TNAESLDGIKSVIAGGVSSSMRAAAVPLPLVVRSAGGCLLRDVEDGEIID
LNMGYGPHLFGYADREVLDAVADQFAKGHMTGLPHELDARAGALIAELVP
GVEQVRFANSGTEAVASALRLARATTGRTLVVTFEGHYHGWSETVLRATR
PTDVVPGALGMIPEALAHTVQLGWNDPDALRELFARDGDRIAAVIVEPVL
ANAGVIPPAPGFLQLLRELTGRSGAMLVFDEVITGFRVARGGAQERYGVE
PDLTVLSRVMGGGFPVAAFGGRRHAMRMLASNEAHHAGVYAGNHAALRAV
VAMLGKIRSLPDLYERLEDTGQYMEDTVREVFATEKRPVHINRVGTLMSV
ALLKGSAEPSAEPRDLRQLAALVDFPRHRRLQTLAQKEGVYFHPNALEPW
FLSTAHTRDVIDKVAGALQRSLVGL
3D structure
PDB4zm4 Mechanism-Based Trapping of the Quinonoid Intermediate by Using the K276R Mutant of PLP-Dependent 3-Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin.
ChainE
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V26 Y147 E215 D248 I251 R276 P417
Catalytic site (residue number reindexed from 1) V17 Y138 E197 D230 I233 R258 P399
Enzyme Commision number ?
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 P3B E S28 R31 G120 T121 Y147 G149 N220 D248 V250 R276 S19 R22 G111 T112 Y138 G140 N202 D230 V232 R258
BS02 PLP E G306 V307 G288 V289
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4zm4, PDBe:4zm4, PDBj:4zm4
PDBsum4zm4
PubMed26426567
UniProtA8R0K5

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