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4I0C

The structure of the camelid antibody cAbHuL5 in complex with human lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019730biological_processantimicrobial humoral response
A0031640biological_processkilling of cells of another organism
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
B0003796molecular_functionlysozyme activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006954biological_processinflammatory response
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019730biological_processantimicrobial humoral response
B0031640biological_processkilling of cells of another organism
B0035578cellular_componentazurophil granule lumen
B0035580cellular_componentspecific granule lumen
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0070062cellular_componentextracellular exosome
B1904724cellular_componenttertiary granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
AGLY72
BASN66

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
AARG101
AARG101

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AARG21
DHOH218
DHOH238

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
AALA108
AHOH390
AHOH391
AGLN58
AASN60

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 201
ChainResidue
BLYS33
BHOH370
CSER125
CSER126
CHOH318

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 202
ChainResidue
BGLN58
BILE59
BASN60
BTRP64
BALA108
BTRP109
BHOH358

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 201
ChainResidue
CLYS97
CSER102
CSER105

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 202
ChainResidue
BARG119
BGLN123
CTHR123

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. ChlsCsaLlqdNIadavaC
ChainResidueDetails
ACYS77-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP53
BGLU35
BASP53

219140

PDB entries from 2024-05-01

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