Structure of PDB 3brm Chain A

Receptor sequence
>3brmA (length=290) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
NPALQLHDWVEYYRPFAANGQSAPALGKNDSQLGICVLEPDGTMIHAGDW
NVSFTMQSISKVISFIAACMSRGIPYVLDRVDVEPKPFNPMINAGALTIA
SILPGESAYEKLEFLYSVMETLIGKRPRIHEEVFRSEWETAHRNRALAYY
LKETNFLEAEVEETLEVYLKQCAMESTTEDIALIGLILAHDGYHPIRHEQ
VIPKDVAKLAKALMLTCGMYNASGKYAAFVGVPAKSGVSGGIMALVPPSQ
PFQSGCGIGIYGPAIDEYGNSLTGGMLLKHMAQEWELSIF
3D structure
PDB3brm Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.
ChainA
Resolution2.29 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) S74 K77 Y201 Y253 V271
Catalytic site (residue number reindexed from 1) S58 K61 Y168 Y220 V238
Enzyme Commision number 3.5.1.2: glutaminase.
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 ONL A Q73 S74 N126 E170 Y201 Y253 G270 V271 Q57 S58 N93 E137 Y168 Y220 G237 V238
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006537 glutamate biosynthetic process
GO:0006541 glutamine metabolic process
GO:0006543 glutamine catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3brm, PDBe:3brm, PDBj:3brm
PDBsum3brm
PubMed18459799
UniProtO31465|GLSA1_BACSU Glutaminase 1 (Gene Name=glsA1)

[Back to BioLiP]