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4MTH

Crystal structure of mature human RegIIIalpha

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0006953biological_processacute-phase response
A0007157biological_processheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
A0007165biological_processsignal transduction
A0008284biological_processpositive regulation of cell population proliferation
A0009609biological_processresponse to symbiotic bacterium
A0009611biological_processresponse to wounding
A0010838biological_processpositive regulation of keratinocyte proliferation
A0030246molecular_functioncarbohydrate binding
A0038023molecular_functionsignaling receptor activity
A0042802molecular_functionidentical protein binding
A0042834molecular_functionpeptidoglycan binding
A0043434biological_processresponse to peptide hormone
A0045617biological_processnegative regulation of keratinocyte differentiation
A0050728biological_processnegative regulation of inflammatory response
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0070492molecular_functionoligosaccharide binding
A0090303biological_processpositive regulation of wound healing
A0106015biological_processnegative regulation of inflammatory response to wounding
A2000972biological_processpositive regulation of detection of glucose
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS107
AGLU121
AASP175
AHOH335

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 202
ChainResidue
AHOH447
AHOH473
AHIS50
AHOH318
AHOH354
AHOH413
AHOH444

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 203
ChainResidue
AHIS145
AHOH465
AHOH469

Functional Information from PROSITE/UniProt
site_idPS00615
Number of Residues26
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CAslsrstaflr..WKDYNCnvrlp.YVC
ChainResidueDetails
ACYS146-CYS171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24256734, ECO:0007744|PDB:4MTH
ChainResidueDetails
AHIS50
AHIS107
AGLU121
AHIS145

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PDB entries from 2024-06-12

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