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4PRU

Crystal structure of dimethyllysine hen egg-white lysozyme in complex with sclx4 at 2.2 A resolution

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 Residues16
DetailsBINDING SITE FOR RESIDUE T3Y A 201
ChainResidue
ATYR23
AHOH347
BARG5
BMLY33
BPHE38
BPRO70
BGLY71
BTRP123
AASN106
ATRP111
AARG112
AMLY116
AGLY117
AGOL203
AHOH310
AHOH327

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE T3Y A 202
ChainResidue
ADM01
APHE3
AGLU7
AALA10
AALA11
AARG14
AHIS15
AARG128
AHOH306
AHOH340
AHOH346

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
AASN27
ACYS115
AGLY117
ATHR118
AVAL120
AT3Y201
BARG114

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
APHE34
AARG114
ATHR118
AASP119
ATRP123
BT3Y201

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE T3Y B 201
ChainResidue
AARG5
AMLY33
AGLY71
ASER72
AARG73
ATRP123
AGOL204
AHOH312
BASN106
BTRP111
BARG112
BMLY116
BGLY117
BHOH303
BHOH304
BHOH321
BHOH327
BHOH333
BHOH337

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE T3Y B 202
ChainResidue
BDM01
BPHE3
BGLU7
BALA10
BALA11
BARG14
BHIS15
BHOH311
BHOH316
BHOH346
BHOH347

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

220113

PDB entries from 2024-05-22

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