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4N0J

Crystal structure of dimethyllysine hen egg-white lysozyme in complex with sclx4 at 1.9 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 Residues20
DetailsBINDING SITE FOR RESIDUE T3Y A 201
ChainResidue
ATYR23
BARG5
BMLY33
BPHE38
BPRO70
BGLY71
BTRP123
BHOH336
BHOH338
BHOH383
BHOH390
AASN106
BHOH392
ATRP111
AARG112
AMLY116
AGLY117
AGOL204
AHOH326
AHOH370

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE T3Y A 202
ChainResidue
ADM01
APHE3
AGLU7
AALA10
AALA11
AARG14
AHIS15
AHOH330
AHOH331
AHOH332
AHOH353
AHOH354
AHOH355
AHOH364
AHOH365

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

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
AASN27
AGLY117
ATHR118
AT3Y201
AHOH306
BARG114

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
ADM01
AGLY16
AASP18
AASN19
ATYR20
AGLN41

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 206
ChainResidue
APHE34
AARG114
ATHR118
AASP119
AALA122
ATRP123
BT3Y201

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 207
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH308
AHOH338

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 208
ChainResidue
AGLU35
AHOH317
AHOH321
AHOH325
AHOH385
AHOH387

site_idAC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE T3Y B 201
ChainResidue
AARG5
AMLY33
AGLY71
ASER72
AARG73
AALA122
ATRP123
AGOL206
AHOH314
AHOH318
AHOH384
BASN106
BTRP111
BARG112
BMLY116
BGLY117
BGOL205
BHOH301
BHOH306
BHOH315
BHOH323
BHOH350

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE T3Y B 202
ChainResidue
BHOH343
BHOH344
BHOH378
BHOH396
BDM01
BPHE3
BGLU7
BALA10
BALA11
BARG14
BHIS15
BHOH333

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 203
ChainResidue
BGLY4
BARG5
BCYS6
BGLU7

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 204
ChainResidue
BSER24
BGLY26
BGLN121
BGOL206
BHOH352

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 205
ChainResidue
APHE34
AARG114
BASN27
BMLY116
BGLY117
BT3Y201
BHOH388

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 206
ChainResidue
BMLY13
BASP18
BSER24
BGLN121
BILE124
BCL204

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 207
ChainResidue
BGLU35
BHOH357
BHOH358
BHOH391
BHOH394
BHOH395

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

219515

PDB entries from 2024-05-08

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