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4GCB

100K X-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to HEWL

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 CL A 201
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 202
ChainResidue
ATRP108
AGLN57
AILE58
AASN59
ATRP63

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 204
ChainResidue
ATYR23
AASN113

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 205
ChainResidue
APHE38

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 206
ChainResidue
AASN65
APRO79

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 207
ChainResidue
AASN74

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPT A 208
ChainResidue
AARG14
AHIS15
AASN93

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPT A 209
ChainResidue
AARG14
AHIS15
ACL212

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 210
ChainResidue
AASN106
AARG112
AASN113
ALYS116
AHOH306
AHOH367

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 211
ChainResidue
AARG5
AALA122
ATRP123
AHOH403

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 212
ChainResidue
AILE88
ACPT209

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PT A 213
ChainResidue
AARG14
AHIS15
ATHR89

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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