Structure of PDB 5t8t Chain A

Receptor sequence
>5t8tA (length=379) Species: 242231 (Neisseria gonorrhoeae FA 1090) [Search protein sequence]
SEYLFTSESVSEGHPDKVADQVSDAILDAILAQDPKARVAAETLVNTGLC
VLAGEITTTAQVDYIKVARETIKRIGYNSSELGFDANGCAVGVYYDQQSP
DIADLNQGAGDQGLMFGYACDETPTLMPFAIYYSHRLMQRQSELRKDGRL
PWLRPDAKAQLTVVYDSETGKVKRIDTVVLSTQHDPAISQEELSKAVIEQ
IIKPVLPPELLTDETKYLINPTGRFVIGGPQGDCGLTGRKIIVDTYGGAA
PHGGGAFSGKDPSKVDRSAAYACRYVAKNIVAAGLATQCQIQVSYAIGVA
EPTSISIDTFGTGKISEEKLIALVCEHFDLRPKGIVQMLDLLRPIYGKSA
AYGHFGREEPEFTWERTDKAASLKAAAGL
3D structure
PDB5t8t Crystal Structure of a S-adenosylmethionine Synthase from Neisseria gonorrhoeae with bound AMP and Magnesium
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H15 D17 K18 E43 E56 K168 F235 D243 C244 R249 K250 K270 K274 D276
Catalytic site (residue number reindexed from 1) H14 D16 K17 E42 E55 K158 F225 D233 C234 R239 K240 K260 K264 D266
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 AMP A D102 I103 D121 D101 I102 D111
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004478 methionine adenosyltransferase activity
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006556 S-adenosylmethionine biosynthetic process
GO:0006730 one-carbon metabolic process
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:5t8t, PDBe:5t8t, PDBj:5t8t
PDBsum5t8t
PubMed
UniProtQ5FAC0|METK_NEIG1 S-adenosylmethionine synthase (Gene Name=metK)

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