Structure of PDB 1rwh Chain A

Receptor sequence
>1rwhA (length=754) Species: 43663 (Paenarthrobacter aurescens) [Search protein sequence]
PGAAEFAALRNRWVDQITGRNVIQAGDPDFAKAITALNNKAADSLAKLDA
AAGRTSVFTDLSLAKDAEMVTTYTRLSQLATAWATPTAAVFGDAAVLAAI
KAGLADANTLCYNDRKEEVGNWWSWEIGVPRALADAMVLLHAELSAAERT
AYCAAIDHFVPDPWLQFPPKRGKITSVGANRVDLCQGIIIRSLAGEDPTK
LNHAVAGLSQVWQYVTSGDGIFRDGSFIQHSTTPYTGSYGVVLLTGLSKL
FSLLGGTAFEVSDPTRSIFFDAVEGSFAPVMINGAMADAVRGRSISREAN
TGYDLGASAIEAILLLARAMDPATAARWRGLCAGWIARDTYRPILNSASV
PRTALVKQLEATGVAPVAEATGHKLFPAMDRTMHRGPGWALSLALSSNRI
AWYECGNGENNRGYHTGSGMTYFYTSDLGQYDDAFWATANYNRLPGITVD
TTPLPDKVEGQWGAAVPADEWSGATALGEVAAVGQHLVGPGRTGLTARKS
WFVSGDVTVCLGADISTASGAKVETIVDHRNLHQGSNTLTTAAGTIAGTA
GTVEVLGDGRWVHLEGFGGYAMLDDSPLHVLRETRSGSWSGVNINGSATV
QQRNFATLYVNHGVGPVAGSYAYMVAPGASVDLTRKLLEGNKYSVIRNDA
TAQSVEFKTAKTTAATFWKPGMAGDLGASGPACVVFSRHGNELSLAVSEP
TQKAAGLTLTLPEGTWSSVLEGAGTLGTDADGRSTLTLDTTGLSGKTKLI
KLKR
3D structure
PDB1rwh High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism
ChainA
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N183 H233 Y242 R296 E407
Catalytic site (residue number reindexed from 1) N180 H230 Y239 R293 E404
Enzyme Commision number 4.2.2.5: chondroitin AC 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 ASG A W125 Q169 R174 H233 W465 W122 Q166 R171 H230 W462
BS02 GCT A N124 W126 N183 H233 Y242 N410 N121 W123 N180 H230 Y239 N407
BS03 ASG A W126 Y242 R296 R300 W123 Y239 R293 R297
BS04 GAD A R134 V245 N303 R131 V242 N300
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:1rwh, PDBe:1rwh, PDBj:1rwh
PDBsum1rwh
PubMed15003453
UniProtP84141

[Back to BioLiP]