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5CD2

The crystal structure of endo-1,4-D-glucanase from Vibrio fischeri ES114

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 401
ChainResidue
AARG295
AARG299
AASP373
ATYR375
ASER376
ATHR384
AHOH751

site_idAC2
Number of Residues11
Detailsbinding site for residue GOL A 402
ChainResidue
AASP136
ASER137
ATYR203
AHOH516
AHOH537
AHOH556
AHOH669
AHOH730
AHOH795
AGLU75
AALA134

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
AGLU234
ATHR235
ALYS253
ALYS254
AHOH579

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AARG150
ATHR384

site_idAC5
Number of Residues6
Detailsbinding site for residue NI A 405
ChainResidue
AHIS155
AHOH687
AHOH763
AHOH775
AHOH805
AHOH857

Functional Information from PROSITE/UniProt
site_idPS00589
Number of Residues16
DetailsPTS_HPR_SER PTS HPR domain serine phosphorylation site signature. ESdYYyNSVLTLFgLG
ChainResidueDetails
AGLU354-GLY369

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PDB entries from 2024-07-31

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