Structure of PDB 1p7l Chain C

Receptor sequence
>1p7lC (length=383) Species: 562 (Escherichia coli) [Search protein sequence]
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMV
LVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSP
DINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAE
VRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQE
AVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDT
YGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSY
AIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPI
YKETAAYGHFGREHFPWEKTDKAQLLRDAAGLK
3D structure
PDB1p7l Crystal structure of the s-adenosylmethionine synthetase ternary complex: a novel catalytic mechanism of s-adenosylmethionine synthesis from ATP and MET.
ChainC
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H14 D16 K17 E42 E55 K165 F230 D238 C239 R244 K245 K265 K269 D271
Catalytic site (residue number reindexed from 1) H14 D16 K17 E42 E55 K165 F230 D238 C239 R244 K245 K265 K269 D271
Enzyme Commision number 2.5.1.6: methionine adenosyltransferase.
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 SAM C H14 D163 K165 S186 F230 D238 H14 D163 K165 S186 F230 D238
BS02 SAM C E55 Q98 D101 I102 D118 K269 I302 E55 Q98 D101 I102 D118 K269 I302
BS03 PPK C H14 D16 K165 K245 H14 D16 K165 K245
BS04 PPK C D118 G260 K265 D271 D118 G260 K265 D271
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004478 methionine adenosyltransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0030955 potassium ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006556 S-adenosylmethionine biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0033353 S-adenosylmethionine cycle
Cellular Component
GO:0005737 cytoplasm
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:1p7l, PDBe:1p7l, PDBj:1p7l
PDBsum1p7l
PubMed14967023
UniProtP0A817|METK_ECOLI S-adenosylmethionine synthase (Gene Name=metK)

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