Structure of PDB 3t7v Chain A

Receptor sequence
>3t7vA (length=337) Species: 269797 (Methanosarcina barkeri str. Fusaro) [Search protein sequence]
SLGDKVIEGYQLTDNDLRTLLSLESKEGLERLYSAARKVRDHYFGNRVFL
NCFIYFSTYCKNQCSFCYYNCRNEINRYRLTMEEIKETCKTLKGAGFHMV
DLTMGEDPYYYEDPNRFVELVQIVKEELGLPIMISPGLMDNATLLKAREK
GANFLALYQETYDTELYRKLRVGQSFDGRVNARRFAKQQGYCVEDGILTG
VGNDIESTILSLRGMSTNDPDMVRVMTFLPQEGTPLEGFRDKSNLSELKI
ISVLRLMFPKRLIPASLDLEGIDGMVLRLNAGANIVTSILPPDSQLEGVA
NYDRDLEERDRDIKSVVRRLEIMGMKPARQADFEAVL
3D structure
PDB3t7v Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C71 C75 C78 V111 M144 E205 P275
Catalytic site (residue number reindexed from 1) C60 C64 C67 V100 M133 E194 P264
Enzyme Commision number 5.4.99.58: methylornithine synthase.
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 SF4 A C71 N73 C75 C78 N81 R182 C60 N62 C64 C67 N70 R171
BS02 SAM A F77 M115 Y169 E171 R182 L209 F239 L240 Q242 V310 F66 M104 Y158 E160 R171 L198 F228 L229 Q231 V299
BS03 MD0 A F64 D112 S146 Y169 R235 M237 S277 D279 T298 S299 F53 D101 S135 Y158 R224 M226 S266 D268 T287 S288
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0016853 isomerase activity
GO:0016866 intramolecular transferase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0071524 pyrrolysine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3t7v, PDBe:3t7v, PDBj:3t7v
PDBsum3t7v
PubMed22095926
UniProtQ46E78|PYLB_METBF 3-methylornithine synthase (Gene Name=pylB)

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