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5M1Y

The case of 1lkr held at the PDB and its variable amino acid occupancies; re refinement of 4ow9 to correct this

Replaces:  4OW9
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
B0003796molecular_functionlysozyme activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue PT A 201
ChainResidue
AHIS15
AIOD203
AIOD204
ACL217

site_idAC2
Number of Residues4
Detailsbinding site for residue PT A 202
ChainResidue
AIOD205
AIOD206
AIOD207
ACL218

site_idAC3
Number of Residues3
Detailsbinding site for residue IOD A 203
ChainResidue
APT201
ACL217
AHIS15

site_idAC4
Number of Residues4
Detailsbinding site for residue IOD A 204
ChainResidue
AHIS15
AASN93
APT201
ACL217

site_idAC5
Number of Residues3
Detailsbinding site for residue IOD A 205
ChainResidue
AARG128
APT202
ACL218

site_idAC6
Number of Residues2
Detailsbinding site for residue IOD A 206
ChainResidue
APT202
AIOD207

site_idAC7
Number of Residues3
Detailsbinding site for residue IOD A 207
ChainResidue
APT202
AIOD206
ACL218

site_idAC8
Number of Residues1
Detailsbinding site for residue IOD A 208
ChainResidue
AIOD220

site_idAC9
Number of Residues2
Detailsbinding site for residue IOD A 209
ChainResidue
AASN74
BLYS116

site_idAD1
Number of Residues1
Detailsbinding site for residue IOD A 210
ChainResidue
BSER81

site_idAD2
Number of Residues5
Detailsbinding site for residue IOD A 212
ChainResidue
ASER24
AGLY26
AGLN121
AILE124
BGLN41

site_idAD3
Number of Residues5
Detailsbinding site for residue DMS A 214
ChainResidue
AGLN57
AILE58
AASN59
AILE98
AALA107

site_idAD4
Number of Residues4
Detailsbinding site for residue DMS A 215
ChainResidue
AARG5
AALA122
ATRP123
AARG125

site_idAD5
Number of Residues5
Detailsbinding site for residue DMS A 216
ChainResidue
AASP66
ASER81
BARG21
BGLY22
BASN113

site_idAD6
Number of Residues3
Detailsbinding site for residue CL A 217
ChainResidue
APT201
AIOD203
AIOD204

site_idAD7
Number of Residues4
Detailsbinding site for residue CL A 218
ChainResidue
AARG128
APT202
AIOD205
AIOD207

site_idAD8
Number of Residues3
Detailsbinding site for residue IOD A 219
ChainResidue
AARG14
AHIS15
AASP87

site_idAD9
Number of Residues3
Detailsbinding site for residue IOD A 220
ChainResidue
ALYS96
AVAL109
AIOD208

site_idAE1
Number of Residues1
Detailsbinding site for residue IOD A 221
ChainResidue
ATYR23

site_idAE2
Number of Residues1
Detailsbinding site for residue IOD A 222
ChainResidue
AILE78

site_idAE3
Number of Residues2
Detailsbinding site for residue IOD A 223
ChainResidue
ATRP62
AARG73

site_idAE4
Number of Residues4
Detailsbinding site for residue PT B 201
ChainResidue
BHIS15
BIOD202
BIOD203
BCL212

site_idAE5
Number of Residues3
Detailsbinding site for residue IOD B 202
ChainResidue
BARG14
BHIS15
BPT201

site_idAE6
Number of Residues4
Detailsbinding site for residue IOD B 203
ChainResidue
BHIS15
BLYS96
BPT201
BCL212

site_idAE7
Number of Residues1
Detailsbinding site for residue IOD B 204
ChainResidue
ALYS116

site_idAE8
Number of Residues1
Detailsbinding site for residue IOD B 208
ChainResidue
BASN65

site_idAE9
Number of Residues3
Detailsbinding site for residue DMS B 209
ChainResidue
BARG5
BALA122
BTRP123

site_idAF1
Number of Residues5
Detailsbinding site for residue DMS B 210
ChainResidue
BILE58
BASN59
BTRP63
BALA107
BTRP108

site_idAF2
Number of Residues3
Detailsbinding site for residue DMS B 211
ChainResidue
BGLN121
BILE124
BARG125

site_idAF3
Number of Residues5
Detailsbinding site for residue CL B 212
ChainResidue
BHIS15
BLYS96
BPT201
BIOD203
BNA213

site_idAF4
Number of Residues1
Detailsbinding site for residue NA B 213
ChainResidue
BCL212

site_idAF5
Number of Residues1
Detailsbinding site for residue IOD B 214
ChainResidue
BLEU129

site_idAF6
Number of Residues2
Detailsbinding site for residue IOD B 215
ChainResidue
AASN103
AASN106

site_idAF7
Number of Residues1
Detailsbinding site for residue IOD B 216
ChainResidue
BGLY71

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 Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU35
BASP52

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP101
BASP101

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

222926

PDB entries from 2024-07-24

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