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5L3I

Re-refinement of 4dd6; cisplatin coordination chemistry determination at hen egg white lysozyme His15

Replaces:  4DD6
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 DMS A 201
ChainResidue
AARG5
AALA122
ATRP123

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 202
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH327
AHOH336

site_idAC3
Number of Residues4
Detailsbinding site for residue PT A 203
ChainResidue
AHIS15
ACL205
ANH3206
ANH3207

site_idAC4
Number of Residues4
Detailsbinding site for residue PT A 204
ChainResidue
AARG14
AHIS15
ANH3208
ACL212

site_idAC5
Number of Residues5
Detailsbinding site for residue CL A 205
ChainResidue
AHIS15
ATHR89
AASN93
APT203
ANH3207

site_idAC6
Number of Residues3
Detailsbinding site for residue NH3 A 206
ChainResidue
AHIS15
APT203
ANH3207

site_idAC7
Number of Residues3
Detailsbinding site for residue NH3 A 207
ChainResidue
APT203
ACL205
ANH3206

site_idAC8
Number of Residues3
Detailsbinding site for residue NH3 A 208
ChainResidue
AARG14
APT204
ACL212

site_idAC9
Number of Residues2
Detailsbinding site for residue CL A 209
ChainResidue
ALYS33
APHE38

site_idAD1
Number of Residues2
Detailsbinding site for residue CL A 210
ChainResidue
ATYR23
AASN113

site_idAD2
Number of Residues3
Detailsbinding site for residue CL A 211
ChainResidue
ASER24
AGLY26
AGLN121

site_idAD3
Number of Residues6
Detailsbinding site for residue CL A 212
ChainResidue
AHIS15
AASP87
AILE88
ATHR89
APT204
ANH3208

site_idAD4
Number of Residues6
Detailsbinding site for residue DMS A 213
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
AHOH340

site_idAD5
Number of Residues4
Detailsbinding site for residue DMS A 214
ChainResidue
AARG61
ATRP62
AGLY71
AARG73

site_idAD6
Number of Residues1
Detailsbinding site for residue PT A 215
ChainResidue
ALYS1

site_idAD7
Number of Residues1
Detailsbinding site for residue PT A 216
ChainResidue
ALYS96

site_idAD8
Number of Residues5
Detailsbinding site for residue CL A 217
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72

site_idAD9
Number of Residues2
Detailsbinding site for residue PT A 218
ChainResidue
ALYS33
AASN37

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

222926

PDB entries from 2024-07-24

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