Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3B0O

Crystal structure of alpha-lactalbumin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003796molecular_functionlysozyme activity
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005796cellular_componentGolgi lumen
A0005989biological_processlactose biosynthetic process
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0007267biological_processcell-cell signaling
A0032991cellular_componentprotein-containing complex
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
B0000139cellular_componentGolgi membrane
B0003796molecular_functionlysozyme activity
B0004461molecular_functionlactose synthase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005796cellular_componentGolgi lumen
B0005989biological_processlactose biosynthetic process
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0007267biological_processcell-cell signaling
B0032991cellular_componentprotein-containing complex
B0042742biological_processdefense response to bacterium
B0046872molecular_functionmetal ion binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 124
ChainResidue
ALYS79
AASP82
AASP84
AASP87
AASP88
AHOH128

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 124
ChainResidue
BASP87
BASP88
BHOH132
BHOH133
BLYS79
BASP82
BASP84

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CdisCdkFlddDItddimC
ChainResidueDetails
ACYS73-CYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9537992, ECO:0007744|PDB:1A4V
ChainResidueDetails
ATHR38
AGLN39
ALEU81
AASP83
BTHR38
BGLN39
BLEU81
BASP83

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8366079, ECO:0007744|PDB:1HML
ChainResidueDetails
AGLU49
AGLU116
BGLU49
BGLU116

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:8366079, ECO:0000269|PubMed:9537992, ECO:0007744|PDB:1A4V, ECO:0007744|PDB:1HML
ChainResidueDetails
ALYS79
BASP88
AASP82
AASP84
AASP87
AASP88
BLYS79
BASP82
BASP84
BASP87

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
ChainResidueDetails
AASN45
BASN45

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|Ref.9
ChainResidueDetails
AASN71
BASN71

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon