Structure of PDB 4a1o Chain B

Receptor sequence
>4a1oB (length=517) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
RRPIRRALISVYDKTGLVDLAQGLSAAGVEIISTGSTAKTIADTGIPVTP
VEQLTGFPEVLDGRVKTLHPRVHAGLLADLRKSEHAAALEQLGIEAFELV
VVNLYPFSQTVESGASVDDCVEQIDIGGPAMVRAAAKNHPSAAVVTDPLG
YHGVLAALRAGGFTLAERKRLASLAFQHIAEYDIAVASWMQQTLAPEHPV
AAFPQWFGRSWRRVAMLRYGENPHQQAALYGDPTAWPGLAQAEQLHGKDM
SYNNFTDADAAWRAAFDHEQTCVAIIKHANPCGIAISSVSVADAHRKAHE
CDPLSAYGGVIAANTEVSVEMAEYVSTIFTEVIVAPGYAPGALDVLARKK
NIRVLVAAEPLAGGSELRPISGGLLIQQSDQLDAHGDNPANWTLATGSPA
DPATLTDLVFAWRACRAVKSNAIVIAADGATVGVGMGQVNRVDAARLAVE
RGGERVRGAVAASDAFFPFPDGLETLAAAGVTAVVHPGGSVRDEEVTEAA
AKAGVTLYLTGARHFAH
3D structure
PDB4a1o Structural Analyses of a Purine Biosynthetic Enzyme from Mycobacterium Tuberculosis Reveal a Novel Bound Nucleotide.
ChainB
Resolution2.48 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K283 H284 N427 H523
Catalytic site (residue number reindexed from 1) K277 H278 N421 H517
Enzyme Commision number 2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase.
3.5.4.10: IMP cyclohydrolase.
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 AMZ B N427 A471 F472 R519 F521 N421 A465 F466 R513 F515
BS02 PO4 B N427 N446 R447 N421 N440 R441
BS03 AMZ B R224 Y225 S257 N259 H284 E337 R218 Y219 S251 N253 H278 E331
BS04 PO4 B K20 T40 G41 S42 T43 K14 T34 G35 S36 T37
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003937 IMP cyclohydrolase activity
GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4a1o, PDBe:4a1o, PDBj:4a1o
PDBsum4a1o
PubMed21956117
UniProtP9WHM7|PUR9_MYCTU Bifunctional purine biosynthesis protein PurH (Gene Name=purH)

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