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

4XYY

Hen Egg-White Lysozyme (HEWL) complexed with Zr(IV)-substituted Keggin-type polyoxometalate

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 Residues32
Detailsbinding site for residue ZKG A 201
ChainResidue
AGLY16
ALYS96
AHOH301
AHOH301
AHOH303
AHOH304
AHOH304
AHOH307
AHOH307
AHOH309
AHOH309
ATYR20
AHOH312
AHOH312
AHOH320
AHOH320
AHOH323
AHOH323
AHOH357
AHOH374
AHOH389
AHOH389
ATYR20
AHOH409
AHOH423
AHOH423
AARG45
AARG45
AASN46
AASN46
ATHR47
ALYS96

site_idAC2
Number of Residues6
Detailsbinding site for residue DMS A 202
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAC3
Number of Residues7
Detailsbinding site for residue EDN A 203
ChainResidue
ASER24
ALEU25
AGLY26
AVAL120
AGLN121
AILE124
AHOH311

site_idAC4
Number of Residues4
Detailsbinding site for residue EDN A 204
ChainResidue
AARG21
AASN46
ATHR47
AHOH316

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon