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

4HTK

Mitigation of X-ray damage in macromolecular crystallography by submicrometer line focusing; total dose 2.17 x 10e+12 X-ray photons

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
ATYR23
AASN113

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
ASER24
AGLY26
AGLN121
AHOH410

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
ASER72
AGLY67
AARG68
ATHR69

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 204
ChainResidue
AILE88

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 205
ChainResidue
ALYS33
APHE38

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 206
ChainResidue
AASN65
APRO79
AHOH356

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 207
ChainResidue
AARG73
AASN74

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 208
ChainResidue
AALA42
AASN44
AARG68
AHOH350
AHOH443

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 209
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH304
AHOH320

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 210
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
AHOH311
AHOH347
AHOH382

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 211
ChainResidue
AARG5
AHOH381

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 212
ChainResidue
AALA10
AALA11
AALA11
AHOH359
AHOH359
AHOH432
AHOH432

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon