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1HF4

STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME CRYSTALS

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 150
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH2058
AHOH2065

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 150
ChainResidue
BASN74
BHOH2069
BHOH2072
BHOH2076
BSER60
BCYS64
BARG73

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 801
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AHOH2119
BARG112
BLYS116
BHOH2109

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 802
ChainResidue
ALYS1
AGLN41
ASER86
AHOH2120
AHOH2121

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 803
ChainResidue
APHE3
AALA11
AARG14
AHIS15
ASER86
AASP87
AILE88

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 801
ChainResidue
AARG112
ALYS116
BASN65
BASN74
BASN77
BILE78
BPRO79

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 B 802
ChainResidue
BGLY126
BHOH2126
BHOH2127

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 803
ChainResidue
AARG21
AGLY22
BASN65
BASP66
BPRO79
BCYS80
BSER81
BHOH2128

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 804
ChainResidue
BPHE3
BALA11
BARG14
BHIS15
BSER86
BASP87
BILE88
BTHR89
BHOH2084
BHOH2129

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 B 805
ChainResidue
BARG45
BASN46
BTHR47
BGLY49
BHOH2130

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
BGLU35
BASP52

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

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PDB entries from 2024-07-24

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