Structure of PDB 3a8i Chain A

Receptor sequence
>3a8iA (length=363) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AQQTPLYEQHTLCGARMVDFHGWMMPLHYGSQIDEHHAVRTDAGMFDVSH
MTIVDLRGSRTREFLRYLLANDVAKLTKSGKALYSGMLNASGGVIDDLIV
YYFTEDFFRLVVNSATREKDLSWITQHAEPFGIEITVRDDLSMIAVQGPN
AQAKAATLFNDAQRQAVEGMKPFFGVQAGDLFIATTGYTGEAGYEIALPN
EKAADFWRALVEAGVKPCGLGARDTLRLEAGMNLYGQEMDETISPLAANM
GWTIAWEPADRDFIGREALEVQREHGTEKLVGLVMTEKGVLRNELPVRFT
DAQGNQHEGIITSGTFSPTLGYSIALARVPEGIGETAIVQIRNREMPVKV
TKPVFVRNGKAVA
3D structure
PDB3a8i Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism
ChainA
Resolution1.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D97
Catalytic site (residue number reindexed from 1) D97
Enzyme Commision number 2.1.2.10: aminomethyltransferase.
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 C2F A M51 Y84 D97 I99 V111 N113 F173 Y188 E195 R223 M232 W252 M51 Y84 D97 I99 V111 N113 F173 Y188 E195 R223 M232 W252
Gene Ontology
Molecular Function
GO:0004047 aminomethyltransferase activity
GO:0008483 transaminase activity
Biological Process
GO:0006546 glycine catabolic process
GO:0006730 one-carbon metabolic process
GO:0019464 glycine decarboxylation via glycine cleavage system
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005960 glycine cleavage complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3a8i, PDBe:3a8i, PDBj:3a8i
PDBsum3a8i
PubMed20375021
UniProtP27248|GCST_ECOLI Aminomethyltransferase (Gene Name=gcvT)

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