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3TXD

HEWL co-crystallization with carboplatin in aqueous media with glycerol as the cryoprotectant

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1130
ChainResidue
ATYR23
AASN113
AGOL142

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1131
ChainResidue
ASER24
AGLY26
AGLN121
AGOL140

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 1132
ChainResidue
AARG68
ATHR69
ANA131
ANA137
AASN65
AGLY67

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1133
ChainResidue
AILE88

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1134
ChainResidue
APHE38

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1135
ChainResidue
AASN65
APRO79

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1136
ChainResidue
AARG73
AASN74
AGOL130

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1137
ChainResidue
AALA42
AARG68
AHOH2042
AHOH2044

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1138
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AGOL130
ANA131

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
ATRP62
ATRP63
AASP101
AGLN121

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 130
ChainResidue
AASN65
ASER72
AARG73
AASN74
ANA131
ACL1136
ANA1138
AHOH2086

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NA A 131
ChainResidue
ASER60
ACYS64
AASN65
AASP66
ATHR69
ASER72
AGOL130
ACL1132
ANA1138

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 132
ChainResidue
ASER86
AASP87

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 133
ChainResidue
AARG21
AGLY22
AGOL142
AHOH2027
AHOH2056

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 134
ChainResidue
AARG14
AHIS15
AHOH2105

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 135
ChainResidue
AASN93
ALYS97
AGOL139
AHOH2087
AHOH2103

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 136
ChainResidue
AALA107
AVAL109
AARG125

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 137
ChainResidue
APRO70
AGLY71
ACL1132

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 138
ChainResidue
AALA122
ATRP123
AHOH2125
AHOH2130

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 139
ChainResidue
ACYS76
AASN77
ALYS97
AGOL135
AHOH2104

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 140
ChainResidue
ALYS13
AASP18
ALEU25
AILE124
ACL1131

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 141
ChainResidue
ATHR118
AASP119
AVAL120
AGLN121

site_idCC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 142
ChainResidue
AARG21
AGLU35
AGOL133
ACL1130
AHOH2038
AHOH2043
AHOH2068

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 143
ChainResidue
AASN59
ATRP63
AALA107
ATRP108
AHOH2074
AHOH2112
AGLN57
AILE58

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

237992

PDB entries from 2025-06-25

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