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4OXB

Structure of ECP with sulphate anions at 1.50 Angstroms

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0002227biological_processinnate immune response in mucosa
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006401biological_processRNA catabolic process
A0006935biological_processchemotaxis
A0019731biological_processantibacterial humoral response
A0035578cellular_componentazurophil granule lumen
A0042742biological_processdefense response to bacterium
A0043152biological_processinduction of bacterial agglutination
A0045087biological_processinnate immune response
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0001530molecular_functionlipopolysaccharide binding
B0002227biological_processinnate immune response in mucosa
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004540molecular_functionRNA nuclease activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006401biological_processRNA catabolic process
B0006935biological_processchemotaxis
B0019731biological_processantibacterial humoral response
B0035578cellular_componentazurophil granule lumen
B0042742biological_processdefense response to bacterium
B0043152biological_processinduction of bacterial agglutination
B0045087biological_processinnate immune response
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG34
AASN39
AHOH403
AHOH447
AHOH465
AHOH509
BARG104

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG101
AHOH435
AHOH523
AHOH579
AARG1
AARG7

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG77
AARG104
AHOH402
AHOH412
BARG36

site_idAC4
Number of Residues11
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG121
AARG121
AHOH404
AHOH407
AHOH415
AHOH415
AHOH416
AHOH416
BVAL52
BPRO123
BVAL124

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 305
ChainResidue
AARG28
AASN32
AARG61
AARG66
AHOH401
AHOH410

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 A 306
ChainResidue
AARG22
AHOH405
AHOH419
AHOH452
BARG28
BASN32
BARG61
BARG66

site_idAC7
Number of Residues9
Detailsbinding site for residue SO4 B 301
ChainResidue
AARG104
BARG34
BLYS38
BASN39
BHOH408
BHOH409
BHOH418
BHOH422
BHOH529

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 302
ChainResidue
BARG1
BARG7
BARG101
BHOH439

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 B 303
ChainResidue
ATRP35
AARG36
AHOH461
BARG77
BARG104
BHOH403

site_idBC1
Number of Residues7
Detailsbinding site for residue SO4 B 304
ChainResidue
AARG75
AHOH451
BASN87
BPRO88
BGLY89
BHOH406
BHOH428

site_idBC2
Number of Residues6
Detailsbinding site for residue SO4 B 305
ChainResidue
AGLN58
ASER59
AHOH432
BARG97
BHOH433
BHOH493

site_idBC3
Number of Residues8
Detailsbinding site for residue SO4 B 306
ChainResidue
AASN57
AGLN58
AARG75
BASN87
BGLN91
BARG97
BHOH420
BHOH457

site_idBC4
Number of Residues6
Detailsbinding site for residue SO4 B 307
ChainResidue
BASN57
BGLN58
BARG73
BARG75
BARG75
BHOH496

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKnqNTF
ChainResidueDetails
ACYS37-PHE43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS15
BHIS15

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS128
BHIS128

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS38
BLYS38

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: May be involved in LPS-binding
ChainResidueDetails
ATYR33
BTYR33

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: May be involved in LPS- and LTA-binding
ChainResidueDetails
ATRP35
BTRP35

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:18694936
ChainResidueDetails
ATYR33
BTYR33

site_idSWS_FT_FI7
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN57
AASN65
AASN92
BASN57
BASN65
BASN92

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PDB entries from 2024-10-16

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