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1HML

ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005989biological_processlactose biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 124
ChainResidue
AASP87
AASP88
AHOH140
AHOH141
ALYS79
AASP82
AASP84

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 125
ChainResidue
AGLU49
AGLU116
AHOH146
AHOH147

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 139
ChainResidue
AGLN39
AARG70
ALYS94
AHOH154
AHOH217

site_idCA
Number of Residues5
Details
ChainResidue
ALYS79
AASP82
AASP84
AASP87
AASP88

site_idZN
Number of Residues1
Details
ChainResidue
AGLU49

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9537992, ECO:0007744|PDB:1A4V
ChainResidueDetails
ATHR38
AGLN39
ALEU81
AASP83

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8366079, ECO:0007744|PDB:1HML
ChainResidueDetails
AGLU49
AGLU116

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:8366079, ECO:0000269|PubMed:9537992, ECO:0007744|PDB:1A4V, ECO:0007744|PDB:1HML
ChainResidueDetails
ALYS79
AASP82
AASP84
AASP87
AASP88

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
ChainResidueDetails
AASN45

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|Ref.9
ChainResidueDetails
AASN71

224931

PDB entries from 2024-09-11

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