Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5D5F

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0008152biological_processmetabolic process
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase 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 Residues1
Detailsbinding site for residue BR A 201
ChainResidue
ATYR23

site_idAC2
Number of Residues1
Detailsbinding site for residue BR A 202
ChainResidue
AILE88

site_idAC3
Number of Residues3
Detailsbinding site for residue BR A 203
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC4
Number of Residues1
Detailsbinding site for residue BR A 204
ChainResidue
ALYS33

site_idAC5
Number of Residues3
Detailsbinding site for residue BR A 205
ChainResidue
AASN65
AARG68
ATHR69

site_idAC6
Number of Residues4
Detailsbinding site for residue BR A 206
ChainResidue
AALA42
AASN44
AARG68
AHOH370

site_idAC7
Number of Residues1
Detailsbinding site for residue BR A 207
ChainResidue
AASN74

site_idAC8
Number of Residues6
Detailsbinding site for residue NA A 208
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH375
AHOH390

site_idAC9
Number of Residues7
Detailsbinding site for residue ACY A 209
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
AHOH337

site_idAD1
Number of Residues1
Detailsbinding site for residue PE5 A 210
ChainResidue
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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon