Structure of PDB 2brw Chain A Binding Site BS01

Receptor Information
>2brw Chain A (length=721) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VKDTYTDRLDDWNGIIAGNQYYDSKNDQMAKLNQELEGKVADSLSSISSQ
ADRIYLWEKFSNYKTSANLTATYRKLEEMAKQVTNPSSRYYQDETVVRTV
RDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIK
KYTDVIEKFVPDPEHFRKTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQE
ISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQL
LPVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANS
EGHVAAVEVLRGIHRIADMSEGETKQRLQSLVKTIVQSDSYYDVFKNLKT
YKDISLMQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAEKGFGFGLSLF
SSRTLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPG
TTETDAKRADSDTGKVLPSAFVGTSKLDDANATATMDFTNWNQTLTAHKS
WFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESSNPYKVYVNDKEASLT
EQEKDYPETQSVFLESSDSKKNIGYFFFKKSSISMSKALQKGAWKDINEG
QSDKEVENEFLTISQAHKQNGDSYGYMLIPNVDRATFNQMIKELESSLIE
NNETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYK
IAYYNPETQESAPDQEVFKKL
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain2brw Chain A Residue 1891 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2brw Alternate Structural Conformations of Streptococcus Pneumoniae Hyaluronan Lyase: Insights Into Enzyme Flexibility and Underlying Molecular Mechanism of Action.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		H578 K581
Binding residue
(residue number reindexed from 1)		H409 K412
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2brw, PDBe:2brw, PDBj:2brw
PDBsum2brw
PubMed16569416
UniProtQ54873|HYSA_STRPN Hyaluronate lyase (Gene Name=SP_0314)

[Back to BioLiP]