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4YEM

Carboplatin binding to HEWL in NaBr crystallisation conditions studied at an X-ray wavelength of 0.9163A - new refinement

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 Residues5
Detailsbinding site for residue PT A 201
ChainResidue
AHIS15
ABR202
ABR203
ABR204
ACL223

site_idAC2
Number of Residues5
Detailsbinding site for residue BR A 202
ChainResidue
ACL223
AHIS15
AASN93
APT201
ABR204

site_idAC3
Number of Residues4
Detailsbinding site for residue BR A 203
ChainResidue
AARG14
AHIS15
APT201
ACL223

site_idAC4
Number of Residues3
Detailsbinding site for residue BR A 204
ChainResidue
APT201
ABR202
ACL223

site_idAC5
Number of Residues2
Detailsbinding site for residue BR A 205
ChainResidue
AILE88
APT224

site_idAC6
Number of Residues2
Detailsbinding site for residue BR A 206
ChainResidue
ATYR23
AASN113

site_idAC7
Number of Residues3
Detailsbinding site for residue BR A 207
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC8
Number of Residues2
Detailsbinding site for residue BR A 208
ChainResidue
ATHR69
ASER72

site_idAC9
Number of Residues2
Detailsbinding site for residue BR A 210
ChainResidue
ATRP63
ADMS220

site_idAD1
Number of Residues2
Detailsbinding site for residue BR A 212
ChainResidue
APRO70
AHOH324

site_idAD2
Number of Residues2
Detailsbinding site for residue BR A 213
ChainResidue
AARG73
AASN74

site_idAD3
Number of Residues3
Detailsbinding site for residue BR A 214
ChainResidue
ALYS96
AARG128
APT218

site_idAD4
Number of Residues4
Detailsbinding site for residue BR A 215
ChainResidue
AASN65
AASN74
AILE78
APRO79

site_idAD5
Number of Residues1
Detailsbinding site for residue BR A 216
ChainResidue
AASN93

site_idAD6
Number of Residues3
Detailsbinding site for residue BR A 217
ChainResidue
AGLY4
ACYS6
AGLU7

site_idAD7
Number of Residues3
Detailsbinding site for residue PT A 218
ChainResidue
ALYS96
ABR214
AHOH301

site_idAD8
Number of Residues6
Detailsbinding site for residue NA A 219
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH412
AHOH419

site_idAD9
Number of Residues7
Detailsbinding site for residue DMS A 220
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
ABR210

site_idAE1
Number of Residues4
Detailsbinding site for residue DMS A 221
ChainResidue
AARG61
ATRP62
AGLY71
AHOH475

site_idAE2
Number of Residues3
Detailsbinding site for residue ACT A 222
ChainResidue
AARG5
ATRP123
AHOH364

site_idAE3
Number of Residues4
Detailsbinding site for residue CL A 223
ChainResidue
APT201
ABR202
ABR203
ABR204

site_idAE4
Number of Residues4
Detailsbinding site for residue PT A 224
ChainResidue
AARG14
AHIS15
ABR205
AHOH318

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

222624

PDB entries from 2024-07-17

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