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3G4H

Crystal structure of Human Senescence Marker Protein-30 (Zinc Bound)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0001889biological_processliver development
A0001933biological_processnegative regulation of protein phosphorylation
A0004341molecular_functiongluconolactonase activity
A0005509molecular_functioncalcium ion binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006874biological_processintracellular calcium ion homeostasis
A0007283biological_processspermatogenesis
A0008270molecular_functionzinc ion binding
A0010867biological_processpositive regulation of triglyceride biosynthetic process
A0010907biological_processpositive regulation of glucose metabolic process
A0016787molecular_functionhydrolase activity
A0019853biological_processL-ascorbic acid biosynthetic process
A0030234molecular_functionenzyme regulator activity
A0032781biological_processpositive regulation of ATP-dependent activity
A0043066biological_processnegative regulation of apoptotic process
A0045019biological_processnegative regulation of nitric oxide biosynthetic process
A0045723biological_processpositive regulation of fatty acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0050680biological_processnegative regulation of epithelial cell proliferation
A0050848biological_processregulation of calcium-mediated signaling
A0097421biological_processliver regeneration
A1901318biological_processnegative regulation of flagellated sperm motility
A1902679biological_processnegative regulation of RNA biosynthetic process
A1903011biological_processnegative regulation of bone development
A1903052biological_processpositive regulation of proteolysis involved in protein catabolic process
A1903625biological_processnegative regulation of DNA catabolic process
A2000279biological_processnegative regulation of DNA biosynthetic process
B0001822biological_processkidney development
B0001889biological_processliver development
B0001933biological_processnegative regulation of protein phosphorylation
B0004341molecular_functiongluconolactonase activity
B0005509molecular_functioncalcium ion binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006874biological_processintracellular calcium ion homeostasis
B0007283biological_processspermatogenesis
B0008270molecular_functionzinc ion binding
B0010867biological_processpositive regulation of triglyceride biosynthetic process
B0010907biological_processpositive regulation of glucose metabolic process
B0016787molecular_functionhydrolase activity
B0019853biological_processL-ascorbic acid biosynthetic process
B0030234molecular_functionenzyme regulator activity
B0032781biological_processpositive regulation of ATP-dependent activity
B0043066biological_processnegative regulation of apoptotic process
B0045019biological_processnegative regulation of nitric oxide biosynthetic process
B0045723biological_processpositive regulation of fatty acid biosynthetic process
B0046872molecular_functionmetal ion binding
B0050680biological_processnegative regulation of epithelial cell proliferation
B0050848biological_processregulation of calcium-mediated signaling
B0097421biological_processliver regeneration
B1901318biological_processnegative regulation of flagellated sperm motility
B1902679biological_processnegative regulation of RNA biosynthetic process
B1903011biological_processnegative regulation of bone development
B1903052biological_processpositive regulation of proteolysis involved in protein catabolic process
B1903625biological_processnegative regulation of DNA catabolic process
B2000279biological_processnegative regulation of DNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
AGLU18
AASN154
AASP204
AHOH315
AHOH326
AHOH356

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BHOH344
BGLU18
BASN154
BASP204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:23349732
ChainResidueDetails
BASP204
AASP204

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23349732
ChainResidueDetails
BGLU18
BASN154
BASP204
AGLU18
AASN154
AASP204

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BARG101
BASN103
AARG101
AASN103

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BGLU121
AGLU121

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q64374
ChainResidueDetails
BLYS144
BLYS244
BLYS253
ALYS144
ALYS244
ALYS253

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PDB entries from 2024-07-10

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