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4OWB

Cisplatin binding to HEWL under sodium bromide crystallisation conditions

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 Residues7
Detailsbinding site for residue DMS A 201
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AILE98
AALA107
AHOH391

site_idAC2
Number of Residues4
Detailsbinding site for residue DMS A 202
ChainResidue
AILE78
APRO79
AASN65
AASN74

site_idAC3
Number of Residues6
Detailsbinding site for residue ACT A 203
ChainResidue
AGLY67
AARG68
APRO70
AGLY71
AACT204
ABR209

site_idAC4
Number of Residues7
Detailsbinding site for residue ACT A 204
ChainResidue
ATHR69
APRO70
AGLY71
AGLY71
ASER72
AACT203
ABR209

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 205
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH331
AHOH337

site_idAC6
Number of Residues6
Detailsbinding site for residue MEB A 206
ChainResidue
AALA10
AALA10
AALA11
AALA11
AHOH310
AHOH310

site_idAC7
Number of Residues2
Detailsbinding site for residue BR A 207
ChainResidue
ATYR23
AASN113

site_idAC8
Number of Residues5
Detailsbinding site for residue BR A 208
ChainResidue
ASER24
AGLY26
AGLN121
AILE124
AHOH388

site_idAC9
Number of Residues7
Detailsbinding site for residue BR A 209
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72
AACT203
AACT204

site_idAD1
Number of Residues1
Detailsbinding site for residue BR A 210
ChainResidue
ALYS33

site_idAD2
Number of Residues3
Detailsbinding site for residue PT A 211
ChainResidue
AARG14
AHIS15
ABR214

site_idAD3
Number of Residues5
Detailsbinding site for residue BR A 212
ChainResidue
AHIS15
ATHR89
AASN93
APT216
ACL217

site_idAD4
Number of Residues4
Detailsbinding site for residue BR A 213
ChainResidue
AARG14
AHIS15
APT216
ACL217

site_idAD5
Number of Residues3
Detailsbinding site for residue BR A 214
ChainResidue
AHIS15
AILE88
APT211

site_idAD6
Number of Residues2
Detailsbinding site for residue BR A 215
ChainResidue
ACYS6
AARG128

site_idAD7
Number of Residues4
Detailsbinding site for residue PT A 216
ChainResidue
AHIS15
ABR212
ABR213
ACL217

site_idAD8
Number of Residues3
Detailsbinding site for residue CL A 217
ChainResidue
ABR212
ABR213
APT216

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

221051

PDB entries from 2024-06-12

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