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2FBB

Crystal Structure Analysis of Hexagonal Lysozyme

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 131
ChainResidue
ASER60
ACYS64
ASER72
AARG73
ANO3156
AHOH1038

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 132
ChainResidue
ALEU84
ANO3150
ANO3150
AGLN41
AGLN41
ALEU84

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 133
ChainResidue
ANO3153
ANO3153
AHOH1095
AHOH1095
AHOH1126
AHOH1126

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 134
ChainResidue
AARG14
AARG114
ANO3152
AHOH1015
AHOH1128

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 135
ChainResidue
AARG14
AHIS15
ANO3155
ANO3161

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NO3 A 150
ChainResidue
ALYS1
ALYS1
ATHR40
ATHR40
AGLN41
AGLN41
ALEU84
ALEU84
ASER85
ASER85
ASER86
ASER86
ANA132
ANA132
ANO3158
ANO3158

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 151
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7
ANO3160
AHOH1117
AHOH1139

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 152
ChainResidue
AARG14
AHIS15
AGLY16
ALYS96
AARG114
ATHR118
ANA134
AHOH1119
AHOH1128

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NO3 A 153
ChainResidue
ATYR53
AASN65
AASP66
AARG68
APRO79
ACYS80
ASER81
ANA133
ANA133
ANO3162
AHOH1070
AHOH1095
AHOH1095
AHOH1126

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 154
ChainResidue
ASER24
ALEU25
AGLY26
AVAL120
AGLN121
AILE124
AHOH1020

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 155
ChainResidue
AARG5
ALYS33
APHE38
ATRP123
ANA135
AHOH1023
AHOH1033
AHOH1083

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NO3 A 156
ChainResidue
ASER60
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
ANA131
AHOH1038
AHOH1096

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 157
ChainResidue
AALA110
AASN113
AARG114
AHOH1008

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 158
ChainResidue
ALYS1
ALYS1
ASER86
ASER86
ANO3150
ANO3150
AHOH1031
AHOH1031
AHOH1105

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 A 159
ChainResidue
ALYS13
AASP119
AGLN121
AALA122
AARG125
AARG128
ALEU129
AHOH1075
AHOH1081
AHOH1137

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 160
ChainResidue
ACYS6
AGLU7
AARG125
ANO3151
ANO3164
AHOH1079

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 161
ChainResidue
AHIS15
ASER86
AASP87
AILE88
ANA135
AHOH1030

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 162
ChainResidue
ATHR43
AARG45
ATHR51
AARG68
APRO79
ASER81
ANO3153
AHOH1126

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 163
ChainResidue
AARG45
AASN65
AASN74
AASN77
AILE78
APRO79

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 164
ChainResidue
AARG5
AALA10
AARG14
AARG125
AGLY126
ANO3160
AHOH1069
AHOH1106

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 165
ChainResidue
AILE58
AASN59
AALA107
ATRP108
AHOH1159

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
AGLU35
AASP52

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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