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6ADF

Structure of HEWL co-crystallised with TEMED

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase 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 Residues10
Detailsbinding site for residue 9U3 A 201
ChainResidue
AARG5
AHOH515
AGLY117
AALA122
ATRP123
AHOH312
AHOH335
AHOH369
AHOH387
AHOH497

site_idAC2
Number of Residues2
Detailsbinding site for residue PGO A 202
ChainResidue
ATRP62
AASP101

site_idAC3
Number of Residues6
Detailsbinding site for residue PGO A 203
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAC4
Number of Residues7
Detailsbinding site for residue PGO A 204
ChainResidue
AASN46
AASP48
ASER50
AASN59
AARG61
AHOH327
AHOH394

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 205
ChainResidue
ATYR23
AASN113

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 206
ChainResidue
ASER24
AGLY26
AGLN121
AHOH456

site_idAC7
Number of Residues4
Detailsbinding site for residue CL A 207
ChainResidue
AGLY67
AARG68
ATHR69
ASER72

site_idAC8
Number of Residues6
Detailsbinding site for residue NA A 208
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH368
AHOH391

site_idAC9
Number of Residues6
Detailsbinding site for residue ACT A 209
ChainResidue
AARG73
AASN74
ALEU75
AHOH305
AHOH308
AHOH492

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 Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP101

Catalytic Information from CSA
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

225158

PDB entries from 2024-09-18

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