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4LT3

HEWL co-crystallized with Carboplatin in non-NaCl conditions: crystal 2 processed using the XDS software package

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 Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 201
ChainResidue
AARG73
ALEU75
ATRP123
ADMS206

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 202
ChainResidue
ATRP108
AVAL109
ADMS204
AGLU35
AASP52
AGLN57
AASN59
AALA107

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 203
ChainResidue
AASP119

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 204
ChainResidue
AASN59
ATRP62
ATRP63
AMPD202

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 205
ChainResidue
AALA42
AASN44
AARG68
AHOH315
AHOH319

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 206
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7
AARG14
AMPD201

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE QPT A 207
ChainResidue
AHIS15

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE QPT A 208
ChainResidue
AALA11
AARG14
AHIS15
ASER86
AASP87
AILE88

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

226707

PDB entries from 2024-10-30

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