Structure of PDB 1l8n Chain A

Receptor sequence
>1l8nA (length=671) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
GYEPCWLRYERKDQYSRLRFEEIVAKRTSPIFQAAVEELQKGLRSMMEIE
PQVVQEVNETANSIWLGTLEDEEFERPLEGTLVHPEGYVIRSDVDPFRIY
IIGKTDAGVLYGVFHFLRLLQMGENIAQLSIIEQPKNRLRMINHWDNMDG
SIERGYAGRSIFFVDDQFVNQRIKDYARLLASVGINAISINNVNVHKTET
KLITDHFLPDVAEVADIFRTYGIKTFLSINYASPIEIGGLPTADPLDPEV
RWWWKETAKRIYQYIPDFGGFVVKADSEFRPGPFTYGRDHAEGANMLAEA
LAPFGGLVIWRCFVYNCQQDWRDRTTDRAKAAYDHFKPLDGQFRENVILQ
IKNGPMDFQVREPVSPLFGAMPKTNQMMEVQITQEYTGQQKHLCFLIPQW
KEVLDFDTYAKGKGSEVKKVIDGSLFDYRYSGIAGVSNIGSDPNWTGHTL
AQANLYGFGRLAWNPDLSAEEIANEWVVQTFGDDSQVVETISWMLLSSWR
IYENYTSPLGVGWMVNPGHHYGPNVDGYEYSHWGTYHYADRDGIGVDRTV
ATGTGYTAQYFPENAAMYESLDTCPDELLLFFHHVPYTHRLHSGETVIQH
IYNTHFEGVEQAKQLRKRWEQLKGKIDEKRYHDVLERLTIQVEHAKEWRD
VINTYFYRKSGIDDQYGRKIY
3D structure
PDB1l8n Crystal Structures of Geobacillus stearothermophilus {alpha}-Glucuronidase Complexed with Its Substrate and Products: MECHANISTIC IMPLICATIONS.
ChainA
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.131: xylan alpha-1,2-glucuronosidase.
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 XYP A R159 G525 H527 W540 R154 G518 H520 W533
BS02 XYP A E285 Y322 R335 D364 H527 Y535 W540 E278 Y315 R328 D357 H520 Y528 W533
BS03 GCW A W150 E158 R159 N201 K281 R318 F320 K359 D364 E392 W145 E153 R154 N194 K274 R311 F313 K352 D357 E385
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033939 xylan alpha-1,2-glucuronosidase activity
GO:0046559 alpha-glucuronidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1l8n, PDBe:1l8n, PDBj:1l8n
PDBsum1l8n
PubMed14573597
UniProtQ8VVD2

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