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1SQ2

Crystal Structure Analysis of the Nurse Shark New Antigen Receptor (NAR) Variable Domain in Complex With Lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
L0003796molecular_functionlysozyme activity
L0005515molecular_functionprotein binding
L0005576cellular_componentextracellular region
L0005615cellular_componentextracellular space
L0005737cellular_componentcytoplasm
L0005783cellular_componentendoplasmic reticulum
L0016231molecular_functionbeta-N-acetylglucosaminidase activity
L0016798molecular_functionhydrolase activity, acting on glycosyl bonds
L0016998biological_processcell wall macromolecule catabolic process
L0031640biological_processkilling of cells of another organism
L0042742biological_processdefense response to bacterium
L0042802molecular_functionidentical protein binding
L0050829biological_processdefense response to Gram-negative bacterium
L0050830biological_processdefense response to Gram-positive bacterium
L0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
N0042101cellular_componentT cell receptor complex
N0042605molecular_functionpeptide antigen binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL L 130
ChainResidue
LASN44
LARG45
LEDO202
NLYS12
NHOH252
NHOH267

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO L 201
ChainResidue
LPRO79
LHOH262
LASN74
LASN77
LILE78

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO L 202
ChainResidue
LTHR43
LASN44
LARG45
LCL130
LHOH221
LHOH222
LHOH309
NHOH242

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO L 203
ChainResidue
LTHR47
LHOH295
NASN21
NCYS22
NSER65
NPHE66
NSER67
NHOH217

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO N 204
ChainResidue
LALA42
LTHR43
LHOH255
NGLU16
NHOH242

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO L 205
ChainResidue
LTHR47
LPRO79
LSER81
LALA82
LHOH307
NTHR58

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
LCYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
LGLU35
LASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
LASP101

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
LGLU35
LASP52

site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
LGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
LASN46
LASP48
LSER50
LASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
LASN59

222926

PDB entries from 2024-07-24

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