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

2G4N

Anomalous substructure of alpha-lactalbumin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005989biological_processlactose biosynthetic process
A0032355biological_processresponse to estradiol
A0032570biological_processresponse to progesterone
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A1903494biological_processresponse to dehydroepiandrosterone
A1903496biological_processresponse to 11-deoxycorticosterone
B0003796molecular_functionlysozyme activity
B0004461molecular_functionlactose synthase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005989biological_processlactose biosynthetic process
B0032355biological_processresponse to estradiol
B0032570biological_processresponse to progesterone
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B1903494biological_processresponse to dehydroepiandrosterone
B1903496biological_processresponse to 11-deoxycorticosterone
C0003796molecular_functionlysozyme activity
C0004461molecular_functionlactose synthase activity
C0005509molecular_functioncalcium ion binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005989biological_processlactose biosynthetic process
C0032355biological_processresponse to estradiol
C0032570biological_processresponse to progesterone
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C1903494biological_processresponse to dehydroepiandrosterone
C1903496biological_processresponse to 11-deoxycorticosterone
D0003796molecular_functionlysozyme activity
D0004461molecular_functionlactose synthase activity
D0005509molecular_functioncalcium ion binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005989biological_processlactose biosynthetic process
D0032355biological_processresponse to estradiol
D0032570biological_processresponse to progesterone
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D1903494biological_processresponse to dehydroepiandrosterone
D1903496biological_processresponse to 11-deoxycorticosterone
E0003796molecular_functionlysozyme activity
E0004461molecular_functionlactose synthase activity
E0005509molecular_functioncalcium ion binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005989biological_processlactose biosynthetic process
E0032355biological_processresponse to estradiol
E0032570biological_processresponse to progesterone
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
E1903494biological_processresponse to dehydroepiandrosterone
E1903496biological_processresponse to 11-deoxycorticosterone
F0003796molecular_functionlysozyme activity
F0004461molecular_functionlactose synthase activity
F0005509molecular_functioncalcium ion binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0005989biological_processlactose biosynthetic process
F0032355biological_processresponse to estradiol
F0032570biological_processresponse to progesterone
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
F1903494biological_processresponse to dehydroepiandrosterone
F1903496biological_processresponse to 11-deoxycorticosterone
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 201
ChainResidue
CLYS79
CASP82
CASP84
CASP87
CASP88
CHOH210

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 202
ChainResidue
DASP87
DASP88
DHOH212
DLYS79
DASP82
DASP84

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 203
ChainResidue
ALYS79
AASP82
AASP84
AASP87
AASP88

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 204
ChainResidue
BLYS79
BASP82
BASP84
BASP87
BASP88

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA F 205
ChainResidue
FLYS79
FASP82
FASP84
FASP87
FASP88
FHOH211
FHOH212

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 206
ChainResidue
ELYS79
EASP82
EASP84
EASP87
EASP88
EHOH212

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 207
ChainResidue
BGLN2
BGLN2
BGLY35
BGLY35

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 208
ChainResidue
AGLN2
AGLN2
AGLY35
AGLY35

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:8805552, ECO:0007744|PDB:1HFZ
ChainResidueDetails
ALYS79
CASP84
CASP87
CASP88
DLYS79
DASP82
DASP84
DASP87
DASP88
ELYS79
EASP82
EASP84
EASP87
EASP88
FLYS79
FASP82
FASP84
FASP87
FASP88
AASP82
AASP84
AASP87
AASP88
BLYS79
BASP82
BASP84
BASP87
BASP88
CLYS79
CASP82

site_idSWS_FT_FI2
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN45
BASN45
CASN45
DASN45
EASN45
FASN45

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon