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3PSR

HUMAN PSORIASIN (S100A7) CA2+ BOUND FORM (CRYSTAL FORM I)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0001525biological_processangiogenesis
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0008270molecular_functionzinc ion binding
A0008544biological_processepidermis development
A0010820biological_processpositive regulation of T cell chemotaxis
A0030216biological_processkeratinocyte differentiation
A0032496biological_processresponse to lipopolysaccharide
A0035578cellular_componentazurophil granule lumen
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050786molecular_functionRAGE receptor binding
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0062023cellular_componentcollagen-containing extracellular matrix
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071624biological_processpositive regulation of granulocyte chemotaxis
A0090026biological_processpositive regulation of monocyte chemotaxis
A0140486molecular_functionzinc ion sequestering activity
B0000302biological_processresponse to reactive oxygen species
B0001525biological_processangiogenesis
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0008270molecular_functionzinc ion binding
B0008544biological_processepidermis development
B0010820biological_processpositive regulation of T cell chemotaxis
B0030216biological_processkeratinocyte differentiation
B0032496biological_processresponse to lipopolysaccharide
B0035578cellular_componentazurophil granule lumen
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050786molecular_functionRAGE receptor binding
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0062023cellular_componentcollagen-containing extracellular matrix
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0071624biological_processpositive regulation of granulocyte chemotaxis
B0090026biological_processpositive regulation of monocyte chemotaxis
B0140486molecular_functionzinc ion sequestering activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 102
ChainResidue
AASP62
AASN64
AASP66
ALYS68
AGLU73
AHOH269

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 103
ChainResidue
AHIS17
AASP24
BHIS86
BHIS90

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 102
ChainResidue
BASP62
BASN64
BASP66
BLYS68
BGLU73
BHOH270

site_idCAA
Number of Residues5
DetailsREGULATORY CA2+ BINDING SITE
ChainResidue
AASP62
AASN64
AASP66
ALYS68
AGLU73

site_idCAB
Number of Residues5
DetailsREGULATORY CA2+ BINDING SITE
ChainResidue
BGLU73
BASP62
BASN64
BASP66
ALYS68

site_idZNA
Number of Residues4
DetailsZN2+ BINDING SITE
ChainResidue
AHIS17
AASP24
BHIS86
BHIS90

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKNEDKKIDfsEF
ChainResidueDetails
AASP62-PHE74

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. VFekKDkneDkkiDFsEFlsLL
ChainResidueDetails
AVAL57-LEU78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALYS18
ALYS25
ALYS87
AGLY91
BLYS18
BLYS25
BLYS87
BGLY91

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
ALYS63
BPHE74
AGLU65
ALYS67
AILE69
APHE74
BLYS63
BGLU65
BLYS67
BILE69

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:8526920
ChainResidueDetails
AASN2
BASN2

218853

PDB entries from 2024-04-24

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