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2HTX

Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked by Polymerized Glutaraldehyde in Acidic Environment

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 9501
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72
ANA9604

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 9502
ChainResidue
AGLU35
AHOH9626
AHOH9702

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 9603
ChainResidue
ATYR23
AASN113

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 9604
ChainResidue
APRO70
AGLY71
ACL9501
AHOH9681

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 220 A 9130
ChainResidue
ALYS13
ALYS13
APRO70
APRO70
AARG128
ALEU129
ALEU129
AHOH9624

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EDO A 9001
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AILE98
AALA107
ATRP108
AHOH9616
AHOH9617
AHOH9638
AHOH9672

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 9004
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 9014
ChainResidue
AASN37
AASN39
AGLY67
AARG68
AHOH9619

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 9015
ChainResidue
ATRP63
ALYS97
AASP101

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 9016
ChainResidue
AALA11
AALA11
AARG14
AHOH9651
AHOH9651
AHOH9668
AHOH9668

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues128
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
AGLU35
AASP52

site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
AGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN46
AASP48
ASER50
AASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
AASN59

244693

PDB entries from 2025-11-12

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