Structure of PDB 1h18 Chain B

Receptor sequence
>1h18B (length=759) Species: 562 (Escherichia coli) [Search protein sequence]
SELNEKLATAWEGFTKGDWQNEVNVRDFIQKNYTPYEGDESFLAGATEAT
TTLWDKVMEGVKLENRTHAPVDFDTAVASTITSHDAGYINKQLEKIVGLQ
TEAPLKRALIPFGGIKMIEGSCKAYNRELDPMIKKIFTEYRKTHNQGVFD
VYTPDILRCRKSGVLTGLPDAYGRGRIIGDYRRVALYGIDYLMKDKLAQF
TSLQADLENGVNLEQTIRLREEIAEQHRALGQMKEMAAKYGYDISGPATN
AQEAIQWTYFGYLAAVKSQNGAAMSFGRTSTFLDVYIERDLKAGKITEQE
AQEMVDHLVMKLRMVRFLRTPEYDELFSGDPIWATESIGGMGLDGRTLVT
KNSFRFLNTLYTMGPSPEPNMTILWSEKLPLNFKKFAAKVSIDTSSLQYE
NDDLMRPDFNNDDYAIACCVSPMIVGKQMQFFGARANLAKTMLYAINGGV
DEKLKMQVGPKSEPIKGDVLNYDEVMERMDHFMDWLAKQYITALNIIHYM
HDKYSYEASLMALHDRDVIRTMACGIAGLSVAADSLSAIKYAKVKPIRDE
DGLAIDFEIEGEYPQFGNNDPRVDDLAVDLVERFMKKIQKLHTYRDAIPT
QSVLTITSNVVYGKKTGNTPDGRRAGAPFGPGANPMHGRDQKGAVASLTS
VAKLPFAYAKDGISYTFSIVPNALGKDDEVRKTNLAGLMDGYFHHEASIE
GGQHLNVNVMNREMLLDAMENPEKYPQLTIRVSGYAVRFNSLTKEQQQDV
ITRTFTQSM
3D structure
PDB1h18 X-Ray Structure of Pyruvate Formate-Lyase in Complex with Pyruvate and Coa.How the Enzyme Uses the Cys-418 Thiyl Radical for Pyruvate Cleavage
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W333 C418 C419 G734
Catalytic site (residue number reindexed from 1) W333 C418 C419 G734
Enzyme Commision number 2.3.1.54: formate C-acetyltransferase.
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 DTL B E139 K142 E139 K142
BS02 PYR B R176 W333 C418 F432 R435 I606 R176 W333 C418 F432 R435 I606
BS03 DTL B E225 R228 E225 R228
BS04 DTL B H68 A69 P70 Y125 D324 D330 S741 H68 A69 P70 Y125 D324 D330 S741
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0008861 formate C-acetyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006006 glucose metabolic process
GO:0044814 glycolytic fermentation via PFL pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h18, PDBe:1h18, PDBj:1h18
PDBsum1h18
PubMed12163496
UniProtP09373|PFLB_ECOLI Formate acetyltransferase 1 (Gene Name=pflB)

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