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4N1G

Crystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0008218biological_processbioluminescence
A0046872molecular_functionmetal ion binding
B0005509molecular_functioncalcium ion binding
B0008218biological_processbioluminescence
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CEI A 201
ChainResidue
AHIS22
ATRP114
AGLY115
AVAL118
ATYR138
ASER142
AMET171
AHIS175
ATRP179
ATYR190
AHOH301
AMET25
AHOH302
APHE28
ALEU29
AALA46
AILE50
APHE72
ATYR88
ATRP92

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 202
ChainResidue
AASP30
AASN32
AASN34
ALYS36
AGLU41
AHOH376

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 203
ChainResidue
AASP123
AASP125
ASER127
ATHR129
AGLU134
AHOH312

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 204
ChainResidue
AASP159
AASP161
ASER163
AASP165
AGLU170
AHOH336

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CEI B 201
ChainResidue
BHIS22
BMET25
BPHE28
BLEU29
BALA46
BILE50
BTYR88
BTRP92
BTRP114
BGLY115
BVAL118
BTYR138
BSER142
BMET171
BTHR172
BHIS175
BTRP179
BTYR190
BHOH301
BHOH302

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP159
BASP161
BSER163
BASP165
BGLU170
BHOH313

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BASP123
BASP125
BSER127
BTHR129
BGLU134
BHOH317

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 204
ChainResidue
BASP30
BASN32
BASN34
BLYS36
BGLU41
BHOH330

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DINGNGKITldEI
ChainResidueDetails
AASP30-ILE42
AASP123-TRP135
AASP159-MET171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"UniProtKB","id":"P02592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues70
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 768
ChainResidueDetails
AHIS22electrostatic stabiliser, proton acceptor
ATRP92electrostatic stabiliser
ATYR138electrostatic stabiliser
AHIS175electrostatic stabiliser, proton acceptor
ATYR190electrostatic stabiliser, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues5
DetailsM-CSA 768
ChainResidueDetails
BHIS22electrostatic stabiliser, proton acceptor
BTRP92electrostatic stabiliser
BTYR138electrostatic stabiliser
BHIS175electrostatic stabiliser, proton acceptor
BTYR190electrostatic stabiliser, proton acceptor, proton donor, proton relay

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PDB entries from 2025-08-27

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