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5D5C

In meso in situ serial X-ray crystallography structure of lysozyme at 100 K

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 Residues3
Detailsbinding site for residue BR A 201
ChainResidue
ATYR23
AASN113
AHOH374

site_idAC2
Number of Residues2
Detailsbinding site for residue BR A 202
ChainResidue
AARG68
AHOH352

site_idAC3
Number of Residues5
Detailsbinding site for residue BR A 203
ChainResidue
AARG68
AGLN41
AALA42
ATHR43
ATYR53

site_idAC4
Number of Residues3
Detailsbinding site for residue BR A 204
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC5
Number of Residues5
Detailsbinding site for residue BR A 205
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
AHOH341

site_idAC6
Number of Residues4
Detailsbinding site for residue BR A 206
ChainResidue
AGLY22
ASER24
AASN27
AARG114

site_idAC7
Number of Residues2
Detailsbinding site for residue BR A 207
ChainResidue
AASP87
AILE88

site_idAC8
Number of Residues6
Detailsbinding site for residue NA A 208
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH341
AHOH380

site_idAC9
Number of Residues5
Detailsbinding site for residue ACY A 209
ChainResidue
AASN59
ATRP63
AALA107
ATRP108
AHOH338

site_idAD1
Number of Residues2
Detailsbinding site for residue PE5 A 210
ChainResidue
AALA122
ATRP123

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

222624

PDB entries from 2024-07-17

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