Structure of PDB 5a0u Chain G

Receptor sequence
>5a0uG (length=793) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
VMEGLTPRMQRLRNHYLTVRPSVSIYRALAFTEVVKANPGMPTILLRAKA
FRHACETAPILIQDDELIVGHPCGKPRAGAFSPDIAWRWVRDELDTMSTR
PQDPFEISEADKKTIREEIVPFWEGRSLDEICEAQYREAGVWAFSGETFV
SDLSYHQINGGGDTCPGYDVLLFTKGMNGIKADAEAHLASLSMENPEDID
RIYYYKAAIETCEGVVNYARRIAAHARELAAKEQNAQRRAELLTIAEVNE
NVPANPPKTLQEALQSIWTVESLFEIEENQTGLSLGRVDQYCYPMFEADI
REGRLTHDTALELLQAFIIKCAELMWMSSELGAKYFAGYQPFINLTVGGQ
KRSGGDACNDLTYLIMDAVRFVKVYQPSLACRIHNQSPQKYMEKIVDVVK
AGMGFPACHFDDSHIKMMLRKGFDFEDARDYCLMGCVEPQKSGRIYQWTS
TGYTQWPIAIEFVLNRGRMVLFDSYQGLDTGDLRDLRTFDEFDAAVKQQI
AHIVRLSAIGTVISQRVHRDVAPKPLMSLLVEGCMESGKDVAAGGAMVNH
GPGLIFSGLATYVDSMAAIRKLVFEEKKYTLEQIRDALLANFEGYEALRR
DCLNAPKYGNDDNYVDQYALDITEWTEKECRKYKMLYSTLSHGTLSISNN
TPIGELTNATPNGRLAWMPLSDGISPTQGADKQGPTAIIKSVSKMNVETM
NIGMVHNFKFLKGLLDTPEGRHGLITLLRTASILGNGQMQFSYVDNEVLK
KAQQEPEKYRDLIVRVAGYSAYFVELCKEVQDEIISRTVIEKF
3D structure
PDB5a0u Structure and Function of Cutc Choline Lyase from Human Microbiota Bacterium Klebsiella Pneumoniaee
ChainG
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) F677 G770 C771 G1103
Catalytic site (residue number reindexed from 1) F342 G435 C436 G768
Enzyme Commision number 4.3.99.4: choline trimethylamine-lyase.
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 CHT G Y490 D498 F677 C771 E773 T784 Y155 D163 F342 C436 E438 T449
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016840 carbon-nitrogen lyase activity
Biological Process
GO:0042426 choline catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5a0u, PDBe:5a0u, PDBj:5a0u
PDBsum5a0u
PubMed26187464
UniProtA0A0M3KL44

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