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6D6H

Triclinic lysozyme cryocooled to 100 K with 47% MPD as cryoprotectant

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 Residues7
Detailsbinding site for residue NO3 A 201
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AARG112
ALYS116

site_idAC2
Number of Residues9
Detailsbinding site for residue NO3 A 202
ChainResidue
AASN65
AASP66
APRO79
ACYS80
ASER81
AHOH353
AHOH360
AARG21
ATYR53

site_idAC3
Number of Residues7
Detailsbinding site for residue NO3 A 203
ChainResidue
AARG5
ALYS33
APHE38
ATRP62
AARG73
ATRP123
AHOH334

site_idAC4
Number of Residues7
Detailsbinding site for residue NO3 A 204
ChainResidue
AALA11
AARG14
AHIS15
AASP87
AILE88
ATHR89
AHOH386

site_idAC5
Number of Residues8
Detailsbinding site for residue NO3 A 205
ChainResidue
ASER24
ALEU25
AGLY26
AGLN41
AGLN121
AILE124
AHOH317
AHOH397

site_idAC6
Number of Residues6
Detailsbinding site for residue NO3 A 206
ChainResidue
ATYR23
AARG45
AMET105
AASN106
ATRP111
AHOH330

site_idAC7
Number of Residues7
Detailsbinding site for residue NO3 A 207
ChainResidue
ATYR20
AARG21
AVAL109
AALA110
AASN113
AARG114
AHOH361

site_idAC8
Number of Residues9
Detailsbinding site for residue MRD A 208
ChainResidue
AGLN57
AASN59
ATRP63
AALA107
AARG128
AHOH324
AHOH356
AHOH390
AHOH396

site_idAC9
Number of Residues16
Detailsbinding site for residue MRD A 209
ChainResidue
ATHR43
AASN44
AARG45
ACYS76
AASN77
AILE78
AASN93
AGLY117
AHOH313
AHOH316
AHOH351
AHOH355
AHOH366
AHOH391
AHOH398
AHOH408

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

218196

PDB entries from 2024-04-10

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