Structure of PDB 5nxa Chain H

Receptor sequence
>5nxaH (length=477) Species: 63221 (Homo sapiens neanderthalensis) [Search protein sequence]
GSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPI
TDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIH
LGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGF
THFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQAS
FLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLAS
LGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSL
ARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQN
ISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLS
QQAASVVKQEGGDNDLIERIQADAYFSPIHSQLDHLLDPSSFTGRASQQV
QRFLEEEVYPLLKPYESVMKVKAELCL
3D structure
PDB5nxa Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase.
ChainH
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H86 T158 H159 S290 K295 E302
Catalytic site (residue number reindexed from 1) H79 T151 H152 S283 K288 E295
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
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 FUM H H86 T111 S112 Q241 H79 T104 S105 Q234
BS02 SSS H T158 H159 T151 H152
BS03 SSS H R20 Y21 S289 S290 M292 K295 M299 R303 R13 Y14 S282 S283 M285 K288 M292 R296
BS04 AMZ H R85 H86 D87 S112 Q241 R329 L331 S334 A335 R338 R78 H79 D80 S105 Q234 R322 L324 S327 A328 R331
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0016829 lyase activity
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5nxa, PDBe:5nxa, PDBj:5nxa
PDBsum5nxa
PubMed30573755
UniProtA0A384E0N4

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