Structure of PDB 2brw Chain A

Receptor sequence

>2brwA (length=721) Species: 1313 (Streptococcus pneumoniae)

VKDTYTDRLDDWNGIIAGNQYYDSKNDQMAKLNQELEGKVADSLSSISSQ
ADRIYLWEKFSNYKTSANLTATYRKLEEMAKQVTNPSSRYYQDETVVRTV
RDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIK
KYTDVIEKFVPDPEHFRKTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQE
ISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQL
LPVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANS
EGHVAAVEVLRGIHRIADMSEGETKQRLQSLVKTIVQSDSYYDVFKNLKT
YKDISLMQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAEKGFGFGLSLF
SSRTLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPG
TTETDAKRADSDTGKVLPSAFVGTSKLDDANATATMDFTNWNQTLTAHKS
WFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESSNPYKVYVNDKEASLT
EQEKDYPETQSVFLESSDSKKNIGYFFFKKSSISMSKALQKGAWKDINEG
QSDKEVENEFLTISQAHKQNGDSYGYMLIPNVDRATFNQMIKELESSLIE
NNETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYK
IAYYNPETQESAPDQEVFKKL

3D structure

• PDB: 2brw Alternate Structural Conformations of Streptococcus Pneumoniae Hyaluronan Lyase: Insights Into Enzyme Flexibility and Underlying Molecular Mechanism of Action.
• Chain: A
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N349 H399 Y408 R462 E577
• Catalytic site (residue number reindexed from 1): N180 H230 Y239 R293 E408
• 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	SO4	A	H578 K581	H409 K412

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:2brw, PDBe:2brw, PDBj:2brw
• PDBsum: 2brw
• PubMed: 16569416
• UniProt: Q54873|HYSA_STRPN Hyaluronate lyase (Gene Name=SP_0314)