Structure of PDB 3q8n Chain D

Receptor sequence
>3q8nD (length=439) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
TLTQERRLVTAIPGPISQELQARKQSAVAAGVGVTLPVYVVAAGGGVLAD
ADGNQLIDFGSGIAVTTVGNSAPAVVDAVTQQVAAFTHTCFMVTPYEGYV
KVAEHLNRLTPGDHEKRTALFNSGAEAVENAVKIARAYTRRQAVVVFDHA
YHGRTNLTMAMTAKNQPYKHGFGPFANEVYRVPTSYPFRDGETDGAAAAA
HALDLINKQVGADNVAAVVIEPVHGEGGFVVPAPGFLGALQKWCTDNGAV
FVADEVQTGFARTGALFACEHENVVPDLIVTAKGIAGGLPLSAVTGRAEI
MDGPQSGGLGGTYGGNPLACAAALAVIDTIERENLVARARAIGETMLSRL
GALAAADPRIGEVRGRGAMIAVELVKPGTTEPDADLTKRVAAAAHAQGLV
VLTCGTYGNVLRFLPPLSMPDHLLDEGLDILAAVFAEVK
3D structure
PDB3q8n Increasing the structural coverage of tuberculosis drug targets.
ChainD
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V42 Y161 E231 D264 Q267 K293 T322 R422
Catalytic site (residue number reindexed from 1) V32 Y151 E221 D254 Q257 K283 T312 R412
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate transaminase.
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 SSN D G134 A135 H162 V266 G124 A125 H152 V256
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042802 identical protein binding
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3q8n, PDBe:3q8n, PDBj:3q8n
PDBsum3q8n
PubMed25613812
UniProtA0QQ04

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