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1CB8

CHONDROITINASE AC LYASE FROM FLAVOBACTERIUM HEPARINUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016829molecular_functionlyase activity
A0030246molecular_functioncarbohydrate binding
A0030341molecular_functionchondroitin AC lyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idACT
Number of Residues3
DetailsHYPOTHETICAL ACTIVE SITE WITH THE HIS SERVING AS THE CATALYTIC BASE
ChainResidue
AHIS225
AARG288
AARG292

site_idCAL
Number of Residues6
DetailsCALCIUM BINDING SITE IN THE BETA-SHEET DOMAIN
ChainResidue
AGLU405
AASP407
ATYR417
AASP416
AHOH3312
AHOH3313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE:
ChainResidueDetails
AHIS225
ATYR234
AARG288

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLU405
AASP407
AASP416
ATYR417

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) serine
ChainResidueDetails
ASER328
ASER455

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10329169
ChainResidueDetails
ATYR234
AHIS225
AARG288

site_idMCSA1
Number of Residues5
DetailsM-CSA 441
ChainResidueDetails
AASN175electrostatic stabiliser
AHIS225electrostatic stabiliser, modifies pKa
ATYR234proton shuttle (general acid/base)
AARG288electrostatic stabiliser, modifies pKa
AGLU371modifies pKa

223532

PDB entries from 2024-08-07

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