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1QBA

BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030203biological_processglycosaminoglycan metabolic process
A0030246molecular_functioncarbohydrate binding
A0030247molecular_functionpolysaccharide binding
A0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ATHR109
AARG454
APHE496
AASN497
AARG498
AGLN499
AHOH1317

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AALA119
ALYS120
ALYS104
ATHR118

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
APRO339
ALYS371
AARG633
ATYR730
AARG825
AHOH1286
AHOH1493

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AHIS107
AARG545
AHOH1568

Functional Information from PROSITE/UniProt
site_idPS00041
Number of Residues46
DetailsHTH_ARAC_FAMILY_1 Bacterial regulatory proteins, araC family signature. KLepTAkfSgfpagkaveIpVVAEYwQLfrndfLprwYATsgDaKP
ChainResidueDetails
ALYS114-PRO159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU540

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Details
ChainResidueDetails
AGLU540
AASP539

site_idMCSA1
Number of Residues2
DetailsM-CSA 899
ChainResidueDetails
AASP539electrostatic stabiliser, modifies pKa, steric role
AGLU540proton shuttle (general acid/base)

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PDB entries from 2024-11-06

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