Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4E3Y

X-ray structure of the Serratia marcescens endonuclease at 0.95 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0005576cellular_componentextracellular region
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2601
ChainResidue
AASN1119
AHOH2701
AHOH2702
AHOH2703
AHOH2704
AHOH2705

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 2602
ChainResidue
AHOH2729
BASP2208
BLYS2212
AALA1169
AASP1191
AARG1213

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG A 2603
ChainResidue
ATHR1035
ALYS1037
ALYS1162
AALA1163
AHOH2781
AHOH2782
AHOH2979
AHOH3023

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2301
ChainResidue
BASN2119
BHOH2401
BHOH2402
BHOH2403
BHOH2404
BHOH2405

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 2302
ChainResidue
AASN1020
BGLY2054
BARG2057
BALA2094
BHOH2475
BHOH2592
BHOH2593
BHOH2630
BHOH2684

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 2303
ChainResidue
AASN1020
BARG2057
BARG2087
BHIS2089
BASN2119
BHOH2401
BHOH2402
BHOH2572
BHOH2712
BHOH2735

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 2304
ChainResidue
BTHR2077
BGLY2078
BARG2087
BHOH2517
BHOH2704

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 2305
ChainResidue
BPRO2051
BARG2131
BILE2134
BASP2135

Functional Information from PROSITE/UniProt
site_idPS01070
Number of Residues9
DetailsNUCLEASE_NON_SPEC DNA/RNA non-specific endonucleases active site. DRGHQaplA
ChainResidueDetails
AASP1086-ALA1094

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10047, ECO:0000269|PubMed:8078761
ChainResidueDetails
AHIS1089
BHIS2089

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASN1119
BASN2119

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 42
ChainResidueDetails
AARG1057electrostatic stabiliser
AHIS1089hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN1110electrostatic stabiliser, increase acidity, increase basicity
AASN1119activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand
AGLU1127electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 42
ChainResidueDetails
BARG2057electrostatic stabiliser
BHIS2089hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN2110electrostatic stabiliser, increase acidity, increase basicity
BASN2119activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand
BGLU2127electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon