Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4PHI

Crystal structure of HEWL with hexatungstotellurate(VI)

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
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
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
C0003796molecular_functionlysozyme activity
C0003824molecular_functioncatalytic activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0016231molecular_functionbeta-N-acetylglucosaminidase activity
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016998biological_processcell wall macromolecule catabolic process
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0042802molecular_functionidentical protein binding
C0050829biological_processdefense response to Gram-negative bacterium
C0050830biological_processdefense response to Gram-positive bacterium
C0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
D0003796molecular_functionlysozyme activity
D0003824molecular_functioncatalytic activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0016231molecular_functionbeta-N-acetylglucosaminidase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0016998biological_processcell wall macromolecule catabolic process
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
D0042802molecular_functionidentical protein binding
D0050829biological_processdefense response to Gram-negative bacterium
D0050830biological_processdefense response to Gram-positive bacterium
D0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue TEW A 201
ChainResidue
AASN65
AHOH428
AHOH443
AHOH471
BGLY4
BARG5
BCYS6
DLYS1
DVAL2
DGLN41
AASN74
AILE78
APRO79
AHOH321
AHOH368
AHOH409
AHOH419
AHOH424

site_idAC2
Number of Residues9
Detailsbinding site for residue TEW A 202
ChainResidue
AARG125
AGLY126
ACYS127
AHOH302
AHOH310
AHOH418
AHOH463
BASN113
CARG125

site_idAC3
Number of Residues2
Detailsbinding site for residue NA A 203
ChainResidue
AILE88
AHOH464

site_idAC4
Number of Residues1
Detailsbinding site for residue GOL A 204
ChainResidue
AGLY71

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 205
ChainResidue
ATRP62
AARG73
AHOH451

site_idAC6
Number of Residues20
Detailsbinding site for residue TEW B 201
ChainResidue
BLYS1
BVAL2
BGLN41
BSER86
BHOH306
BHOH322
BHOH325
BHOH342
BHOH394
BHOH409
BHOH424
BHOH434
BHOH438
BHOH440
BHOH451
BHOH462
BHOH467
CASN65
CPRO79
DARG5

site_idAC7
Number of Residues17
Detailsbinding site for residue TEW B 202
ChainResidue
BARG45
BTHR47
BGLY49
BARG68
BHOH316
BHOH344
BHOH347
BHOH420
BHOH422
BHOH431
BHOH437
BHOH456
CHOH403
DARG73
DASN74
DLEU75
DHOH306

site_idAC8
Number of Residues19
Detailsbinding site for residue TEW B 203
ChainResidue
BASN65
BASN74
BILE78
BPRO79
BHOH304
BHOH309
BHOH310
BHOH311
BHOH326
BHOH400
BHOH404
BHOH408
BHOH428
CLYS1
CVAL2
CGLN41
DTEW201
DHOH301
DHOH304

site_idAC9
Number of Residues13
Detailsbinding site for residue TEW B 204
ChainResidue
BHOH433
DASN106
DLYS116
AARG112
ALYS116
BARG73
BLYS116
BGLY117
BTEW205
BHOH307
BHOH308
BHOH318
BHOH330

site_idAD1
Number of Residues15
Detailsbinding site for residue TEW B 205
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7
BARG73
BASN74
BLEU75
BASN77
BLYS97
BTEW204
BHOH302
BHOH318
BHOH327
BHOH329
BHOH436

site_idAD2
Number of Residues2
Detailsbinding site for residue NA B 206
ChainResidue
BHOH453
CARG45

site_idAD3
Number of Residues5
Detailsbinding site for residue NA B 207
ChainResidue
BASN59
BTRP63
BHOH358
BHOH439
BHOH468

site_idAD4
Number of Residues2
Detailsbinding site for residue NA C 201
ChainResidue
AHOH363
CHOH424

site_idAD5
Number of Residues4
Detailsbinding site for residue NA C 202
ChainResidue
CASP87
CILE88
CHOH417
CHOH418

site_idAD6
Number of Residues22
Detailsbinding site for residue TEW D 201
ChainResidue
ALYS1
AVAL2
AGLN41
BTEW203
BHOH310
DASN65
DASN74
DILE78
DPRO79
DHOH301
DHOH302
DHOH303
DHOH304
DHOH307
DHOH309
DHOH311
DHOH317
DHOH340
DHOH370
DHOH377
DHOH401
DHOH437

site_idAD7
Number of Residues4
Detailsbinding site for residue NA D 202
ChainResidue
BHOH338
DGLU7
DARG14
DHOH328

site_idAD8
Number of Residues4
Detailsbinding site for residue ACT D 203
ChainResidue
DASN59
DTRP63
DALA107
DTRP108

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 Residues8
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU35
BASP52
CGLU35
CASP52
DGLU35
DASP52

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP101
BASP101
CASP101
DASP101

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
BGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN46
BASP48
BSER50
BASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
BASN59

site_idMCSA3
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
CGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CASN46
CASP48
CSER50
CASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
CASN59

site_idMCSA4
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
DGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DASN46
DASP48
DSER50
DASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
DASN59

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon