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3AJN

Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis

Replaces:  2ZXS
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
A0008152biological_processmetabolic process
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 Residues4
DetailsBINDING SITE FOR RESIDUE GM1 A 130
ChainResidue
ATRP62
ATRP63
AASP101
AGLN121

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GM1 A 131
ChainResidue
AHOH264
AASN19
AARG21
AGLY22
AASN44
AHOH187

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GM1 A 132
ChainResidue
AASN19
AGLY22
ALYS33
APHE34
AGLU35
ASER36
AASN37
AHOH152
AHOH248
AHOH288
AHOH295

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GM1 A 133
ChainResidue
AASP52
AGLN57
AILE58
AASN59
AALA107
ATRP108
AHOH185
AHOH259

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 134
ChainResidue
ATYR23
AASN113

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 135
ChainResidue
ASER24
AGLY26
AGLN121
AHOH138

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 136
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH177
AHOH186

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

218500

PDB entries from 2024-04-17

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