Structure of PDB 2q1f Chain B

Receptor sequence
>2q1fB (length=991) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
AQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNG
RLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKC
ASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPDAKGRLFIDHL
ITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDKQ
RQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPV
FMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSP
IRKEMRRKFLAMYDHITDQGVAYGSCWGNIHHYGYSVRGLYPAYFLMKDV
LREEGKLLEAERTLRWYAITNEVYPKPEGNGIDMDSFNTQTTGRIASILM
MEDTPEKLQYLKSFSRWIDYGCRPAPGLAGSFKVDGGAFHHRNNYPAYAV
GGLDGATNMIYLFSRTSLAVSELAHRTVKDVLLAMRFYCNKLNFPLSMSG
RHPDGKGKLVPMHYAIMAIAGTPDGKGDFDKEMASAYLRLVSSDMPKVSN
AQERKIAKRLVENGFRAEPDPQGNLSLGYGCVSVQRRENWSAVARGHSRY
LWAAEHYLGHNLYGRYLAHGSLQILTAPPGQTVTPTTSGWQQEGFDWNRI
PGVTSIHLPLDLLKANVLNVDTFSGMEEMLYSDEAFAGGLSQGKMNGNFG
MKLHEHDKYNGTHRARKSFHFIDGMIVCLGSDIENTNMDYPTETTIFQLA
VTDKAAHDYWKNNAGEGKVWMDHLGTGYYVPVAARFEKNFPQYSRMQDTG
KETKGDWVSLIIDHGKAPKAGSYEYAILPGTDRKTMTAFAKKPAYSVLQQ
DRNAHILESPSDRITSYVLFETPQSLLPGGLLQRTDTSCLVMVRKESADK
VLLTVAQPDLALYRGPSDEAFDKDGKRMERSIYSRPWIDNESGEIPVTVT
LKGRWKVVETPYCKVVSEDKKQTVLRFLCKDGASYEVELEK
3D structure
PDB2q1f Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid.
ChainB
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N393 H454 Y461 K521 E628
Catalytic site (residue number reindexed from 1) N380 H441 Y448 K508 E605
Enzyme Commision number 4.2.2.21: chondroitin-sulfate-ABC exolyase.
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 CA B S24 E26 D50 H53 D161 S11 E13 D37 H40 D148
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0030246 carbohydrate binding
GO:0034000 chondroitin-sulfate-ABC endolyase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006027 glycosaminoglycan 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:2q1f, PDBe:2q1f, PDBj:2q1f
PDBsum2q1f
PubMed18227125
UniProtC5G6D7|CABC2_BACT4 Chondroitin sulfate ABC exolyase (Gene Name=chonabc)

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