Structure of PDB 5giq Chain A

Receptor sequence
>5giqA (length=348) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
SSKMDQLRPVLGRAGVDALWVSAPANVRWLSGFTSAEDGKVLVSPDGATL
YTDARYTVQAQEESSLPQYIARPPATYEHAADTVRGLRVGFEAESLTVAE
LEDLRQAWPNSTLVALRGTLGGLRAVKTPEEIGAIRAAQDLADRVYTEVR
PMIRAGVRELDVAVEIETRLRRAGGESAFELIVASGPNGAKPHGHASKRV
IEDGDLVTIDMGARLGGYNSDMTRTVAVGTPSAEMKRVYDAVLEAEEAAI
AAIRPGVRAADLDKLARDLLTRHGLGEAFHSLGHGVGLEVHEGPGLRGTS
QDVLEAGMVITIEPGAYLPGVGGVRIEDLILVTEDGYEVLSHSAKESV
3D structure
PDB5giq Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D82 H193 D210 D221 T223 H281 H285 H292 E314 Y318 R326 E328
Catalytic site (residue number reindexed from 1) D82 H193 D210 D221 T223 H280 H284 H291 E313 Y317 R325 E327
Enzyme Commision number ?
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 ZN A D221 H285 E314 E328 D221 H284 E313 E327
BS02 ZN A D210 D221 E328 D210 D221 E327
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5giq, PDBe:5giq, PDBj:5giq
PDBsum5giq
PubMed30536999
UniProtQ9RUY4

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