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2PC2

Lysozyme Cocrystallized with Tris-dipicolinate Eu complex

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_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 206
ChainResidue
ASER24
AGLY26
AGLN121
AHOH846

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PDC A 302
ChainResidue
AHOH824
ACYS6
AARG112
ACYS127
AARG128
AHOH719

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PDC A 303
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7
ATYR20
ALYS96
ALYS97
AHOH720
AHOH726
AHOH728
AHOH768

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PDC A 304
ChainResidue
AASN93
ALYS97
AARG112
ALYS116
AARG128
AHOH726
AHOH787
AHOH836

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PDC A 402
ChainResidue
AARG125
AGLY126
AHOH786
AHOH788

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PDC A 403
ChainResidue
ATYR20
AARG21
AARG125
AGLY126
AHOH707
AHOH724
AHOH729
AHOH742
AHOH806
AHOH863
AHOH877

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PDC A 404
ChainResidue
ATYR20
AARG21
AARG125
AGLY126
AHOH707
AHOH724
AHOH729
AHOH742
AHOH806
AHOH863
AHOH877

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PDC A 502
ChainResidue
AARG61
ATRP62
AARG68
AARG73
ALEU84
ASER85
ASER86

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PDC A 503
ChainResidue
AARG68
ASER86
AASN103
AHOH800

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PDC A 504
ChainResidue
ATRP62
AHOH843
AHOH880

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PDC A 602
ChainResidue
AARG21
ASER100
AASP101
AGLY102
AASN103
AGLY104
AALA122
AHOH780
AHOH844

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PDC A 603
ChainResidue
AARG14
AARG21
AGLN121
AARG125
AHOH778
AHOH827

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PDC A 604
ChainResidue
ATYR23
AGLY102
AASN103
AASN106
AHOH823
AHOH831

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PDC A 702
ChainResidue
AARG21
AGLY22
ATYR23
AHOH822
AHOH831
AHOH835

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_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

219869

PDB entries from 2024-05-15

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