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4OWA

Carboplatin binding to HEWL under sodium iodide 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
B0003796molecular_functionlysozyme activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue IOD A 204
ChainResidue
ASER24
AGLY26
AGLN121
AILE124
BGLN41

site_idAC2
Number of Residues1
Detailsbinding site for residue IOD A 205
ChainResidue
AASN74

site_idAC3
Number of Residues3
Detailsbinding site for residue IOD A 206
ChainResidue
AARG112
ALYS116
BPRO79

site_idAC4
Number of Residues2
Detailsbinding site for residue IOD A 208
ChainResidue
AASN106
AQPT220

site_idAC5
Number of Residues3
Detailsbinding site for residue IOD A 209
ChainResidue
AASN106
AQPT220
BIOD204

site_idAC6
Number of Residues1
Detailsbinding site for residue IOD A 210
ChainResidue
AARG112

site_idAC7
Number of Residues3
Detailsbinding site for residue IOD A 211
ChainResidue
AASP119
AGLN121
BASN39

site_idAC8
Number of Residues2
Detailsbinding site for residue IOD A 212
ChainResidue
AHIS15
AQPT221

site_idAC9
Number of Residues2
Detailsbinding site for residue IOD A 213
ChainResidue
AHIS15
AQPT221

site_idAD1
Number of Residues2
Detailsbinding site for residue IOD A 214
ChainResidue
ATYR23
BARG45

site_idAD2
Number of Residues1
Detailsbinding site for residue IOD A 215
ChainResidue
AASN103

site_idAD3
Number of Residues2
Detailsbinding site for residue IOD A 216
ChainResidue
AASP18
BGLN41

site_idAD4
Number of Residues2
Detailsbinding site for residue IOD A 219
ChainResidue
AASP87
AILE88

site_idAD5
Number of Residues3
Detailsbinding site for residue QPT A 220
ChainResidue
AIOD208
AIOD209
BIOD204

site_idAD6
Number of Residues4
Detailsbinding site for residue QPT A 221
ChainResidue
AHIS15
ALYS96
AIOD212
AIOD213

site_idAD7
Number of Residues2
Detailsbinding site for residue DMS A 222
ChainResidue
ATRP62
AARG73

site_idAD8
Number of Residues3
Detailsbinding site for residue DMS A 223
ChainResidue
AARG5
ATRP123
AARG125

site_idAD9
Number of Residues6
Detailsbinding site for residue DMS A 224
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AILE98
ATRP108

site_idAE1
Number of Residues1
Detailsbinding site for residue IOD B 201
ChainResidue
BARG61

site_idAE2
Number of Residues1
Detailsbinding site for residue IOD B 202
ChainResidue
BHOH362

site_idAE3
Number of Residues1
Detailsbinding site for residue IOD B 203
ChainResidue
BASN113

site_idAE4
Number of Residues2
Detailsbinding site for residue IOD B 204
ChainResidue
AIOD209
AQPT220

site_idAE5
Number of Residues1
Detailsbinding site for residue IOD B 207
ChainResidue
ASER81

site_idAE6
Number of Residues4
Detailsbinding site for residue IOD B 208
ChainResidue
BHIS15
BASN93
BIOD212
BQPT214

site_idAE7
Number of Residues3
Detailsbinding site for residue IOD B 209
ChainResidue
BHIS15
BIOD212
BQPT214

site_idAE8
Number of Residues1
Detailsbinding site for residue IOD B 210
ChainResidue
BASN37

site_idAE9
Number of Residues1
Detailsbinding site for residue IOD B 211
ChainResidue
BHOH333

site_idAF1
Number of Residues3
Detailsbinding site for residue IOD B 212
ChainResidue
BIOD208
BIOD209
BQPT214

site_idAF2
Number of Residues4
Detailsbinding site for residue QPT B 214
ChainResidue
BHIS15
BIOD208
BIOD209
BIOD212

site_idAF3
Number of Residues3
Detailsbinding site for residue DMS B 215
ChainResidue
BARG5
BALA122
BTRP123

site_idAF4
Number of Residues6
Detailsbinding site for residue DMS B 216
ChainResidue
BGLN57
BILE58
BASN59
BTRP63
BALA107
BTRP108

site_idAF5
Number of Residues6
Detailsbinding site for residue DMS B 217
ChainResidue
ATHR43
AARG45
AARG68
BGLY22
BTYR23
BHOH356

site_idAF6
Number of Residues2
Detailsbinding site for residue ACT B 218
ChainResidue
BTHR47
BASP48

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 Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU35
BASP52

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP101
BASP101

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
BGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN46
BASP48
BSER50
BASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
BASN59

222926

PDB entries from 2024-07-24

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