Structure of PDB 1lxk Chain A

Receptor sequence

>1lxkA (length=719) Species: 1313 (Streptococcus pneumoniae)

KDTYTDRLDDWNGIIAGNQYYDSKNDQMAKLNQELEGKVADSLSSISSQA
DRIYLWEKFSNYKTSANLTATYRKLEEMAKQVTNPSSRYYQDETVVRTVR
DSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKK
YTDVIEKFVPDPEHFRKTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQEI
SSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAFGNVLIDGLSQLL
PVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSE
GHVAAVEVLRGIHRIADMSEGETKQRLQSLVKTIVQSDSYYDVFKNLKTY
KDISLMQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAEKGFGFGLSLFS
SRTLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPGT
TETDAKRADSDTGKVLPSAFVGTSKLDDANATATMDFTNWNQTLTAHKSW
FMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESSNPYKVYVNDKEASLTE
QEKDYPETQSVFLESSDSKKNIGYFFFKKSSISMSKALQKGAWKDINEGQ
SDKEVENEFLTISQAHKQNGDSYGYMLIPNVDRATFNQMIKELESSLIEN
NETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYKI
AYYNPETQESAPDQEVFKK

3D structure

• PDB: 1lxk Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. Structures of complexes with the substrate.
• Chain: A
• Resolution: 1.53 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N349 H399 F408 R462 E577
• Catalytic site (residue number reindexed from 1): N179 H229 F238 R292 E407
• Enzyme Commision number: 4.2.2.1: hyaluronate 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	BDP	A	N290 W291 W292 N349 H399 F408 R462 N580	N120 W121 W122 N179 H229 F238 R292 N410
BS02	BDP	A	R243 R300 R466 E477	R73 R130 R296 E307

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0016829 lyase activity
• GO:0030246 carbohydrate binding

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:1lxk, PDBe:1lxk, PDBj:1lxk
• PDBsum: 1lxk
• PubMed: 11991948
• UniProt: Q54873|HYSA_STRPN Hyaluronate lyase (Gene Name=SP_0314)