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2VB1

HEWL at 0.65 angstrom 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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 201
ChainResidue
AARG21
AGLY22
AASN65
AASP66
AARG68
APRO79
ACYS80
ASER81
AHOH2153

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
AASN44
AARG45
ACYS76
AASN77
AILE78
AHOH2060
AHOH2154

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
AHOH2155
AHOH2156
AHOH2157
AHOH2165

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AALA122
ATRP123
AHOH2146
AHOH2158
AHOH2159

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 401
ChainResidue
ASER24
ALEU25
AGLY26
AGLN41
AGLN121
AILE124
AHOH2160
AHOH2161

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 402
ChainResidue
AGLU7
AASN46
ATHR47
AASP48
ALYS97
AHOH2162

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 403
ChainResidue
AALA11
AARG14
AHIS15
AASP87
AILE88
AHOH2068
AHOH2163
AHOH2164

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 404
ChainResidue
ATRP62
ATRP63
AASN103
AALA107
AHOH2127
AHOH2132
AHOH2165

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 405
ChainResidue
ALYS33
APHE38
ATRP62
AARG73
ATRP123
AHOH2158
AHOH2166

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 406
ChainResidue
ATYR23
AARG45
AGLY104
AMET105
AASN106
ATRP111
AHOH2100
AHOH2131

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 407
ChainResidue
AARG14
ALYS33
AASN37
ATRP62
AARG73
AHOH2167
AHOH2168

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 408
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AARG112
ALYS116

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 409
ChainResidue
ATYR20
AARG21
APHE34
AALA110
AARG114
AHOH2023
AHOH2037
AHOH2169
AHOH2170

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

226707

PDB entries from 2024-10-30

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