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

2D6B

Novel Bromate Species trapped within a Protein Crystal

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 140
ChainResidue
ATYR23
AASN113
AHOH1092

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 141
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 142
ChainResidue
AARG73
AHOH1010
AHOH1012
ASER60
ACYS64
ASER72

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 202 A 131
ChainResidue
AGLY67
AARG68
ATHR69
APRO70
AGLY71
A202132
AHOH1026
AHOH1155

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 202 A 132
ChainResidue
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
A202131
AHOH1012
AHOH1026
AHOH1033
AHOH1046
AHOH1130

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 202 A 133
ChainResidue
ALYS1
AGLN41
AASN65
APRO79
ASER86
AHOH1022
AHOH1039
AHOH1061
AHOH1182

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 202 A 134
ChainResidue
AGLY4
AARG5
ACYS6
AGLU7
AHOH1168

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 202 A 135
ChainResidue
APHE3
AARG14
ASER86
AILE88
AHOH1070

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 202 A 136
ChainResidue
AASN19
AARG45
AARG68
AHOH1101
AHOH1178
AHOH1234
AHOH1267
AHOH1281

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 202 A 137
ChainResidue
ALYS33
AASN37
A202139
AHOH1020
AHOH1273
AHOH1290

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 202 A 138
ChainResidue
AILE58
AASN59
ATRP63
AALA107
AHOH1090
AHOH1127

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 202 A 139
ChainResidue
AGLY22
ASER24
AASN27
AARG114
A202137
AHOH1236
AHOH1290

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon