Structure of PDB 1nbu Chain F

Receptor sequence
>1nbuF (length=118) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
ADRIELRGLTVHGRHGVYDHERVAGQRFVIDVTVWIDLAEAANSDDLADT
YDYVRLASRAAEIVAGPPRKLIETVGAEIADHVMDDQRVHAVEVAVHKPQ
APIPQTFDDVAVVIRRSR
3D structure
PDB1nbu Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme.
ChainF
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E22 K99
Catalytic site (residue number reindexed from 1) E21 K98
Enzyme Commision number 1.13.11.81: 7,8-dihydroneopterin oxygenase.
4.1.2.25: dihydroneopterin aldolase.
5.1.99.8: 7,8-dihydroneopterin epimerase.
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 PH2 F G17 V18 E22 L72 I73 E74 G16 V17 E21 L71 I72 E73
BS02 PH2 F L48 D53 Y54 V55 L47 D52 Y53 V54
Gene Ontology
Molecular Function
GO:0004150 dihydroneopterin aldolase activity
Biological Process
GO:0006760 folic acid-containing compound metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1nbu, PDBe:1nbu, PDBj:1nbu
PDBsum1nbu
PubMed15876368
UniProtP9WNC5|FOLB_MYCTU Dihydroneopterin aldolase (Gene Name=folB)

[Back to BioLiP]