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3TXK

HEWL co-crystallization with cisplatin in DMSO media with paratone as the cryoprotectant at pH 6.5

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1130
ChainResidue
ATYR23
AGLY104
AASN113

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1131
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1132
ChainResidue
ANA1138
AASP66
ATHR69
ASER72

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1134
ChainResidue
AARG5
APHE38

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1135
ChainResidue
AASN74
AILE78

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1136
ChainResidue
AARG73

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1137
ChainResidue
AARG68
ADMS130

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1138
ChainResidue
ASER60
ACYS64
AASN65
ASER72
AARG73
ACL1132

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 130
ChainResidue
ATHR43
AARG45
AGLY49
ATHR51
ACL1137

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 131
ChainResidue
AASN59
ATRP63
AILE98
AALA107

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPT A 133
ChainResidue
AHIS15
ATHR89
AASN93

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CPT A 134
ChainResidue
AARG14
AHIS15
AASP87
AILE88
ATHR89

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 135
ChainResidue
AALA122
ATRP123
AHOH2052

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

226707

PDB entries from 2024-10-30

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