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1JTP

Degenerate interfaces in antigen-antibody complexes

Functional Information from GO Data
ChainGOidnamespacecontents
L0003796molecular_functionlysozyme activity
L0005539molecular_functionglycosaminoglycan binding
L0005576cellular_componentextracellular region
L0005615cellular_componentextracellular space
L0005737cellular_componentcytoplasm
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
M0003796molecular_functionlysozyme activity
M0005539molecular_functionglycosaminoglycan binding
M0005576cellular_componentextracellular region
M0005615cellular_componentextracellular space
M0005737cellular_componentcytoplasm
M0016798molecular_functionhydrolase activity, acting on glycosyl bonds
M0016998biological_processcell wall macromolecule catabolic process
M0031640biological_processkilling of cells of another organism
M0042742biological_processdefense response to bacterium
M0042802molecular_functionidentical protein binding
M0050829biological_processdefense response to Gram-negative bacterium
M0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP99
ATHR101
AGLY119
AASP121
AHOH510
AHOH537

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BASP121
BHOH511
MHOH559
BASP99
BTHR101
BGLY119

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA L 503
ChainResidue
LSER60
LCYS64
LSER72
LLYS73
LHOH515
LHOH568

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA M 504
ChainResidue
MSER60
MCYS64
MSER72
MLYS73
MHOH520
MHOH533

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA L 505
ChainResidue
ASER105
LGLU35
LFMT406
LHOH526
LHOH550
LHOH551

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 401
ChainResidue
AALA6
ATYR94
ATYR95
ACYS96
AGLY124
AGLY126
ATHR127

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 402
ChainResidue
BALA6
BTYR94
BTYR95
BCYS96
BGLY124
BGLN125
BGLY126
BTHR127
BHOH566

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT M 403
ChainResidue
MASN65
MGLY67
MARG68
MTHR69
MSER72
MHOH520
MHOH533

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT M 404
ChainResidue
BHOH511
MHOH543

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT M 405
ChainResidue
LASN113
LARG114
LHOH540
MARG5
MCYS6
MHOH511

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT L 406
ChainResidue
LGLU35
LVAL109
LALA110
LNA505
LHOH551
LHOH571
LHOH576

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

site_idPS00879
Number of Residues17
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gkereg.VaAINMGGGIT
ChainResidueDetails
AGLY42-THR58

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
MGLU35
MASP52

221716

PDB entries from 2024-06-26

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