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6ZSM

Crystal structure of rsGCaMP double mutant Ile80His/Val116Ile in the ON state (non-illuminated)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0006091biological_processgeneration of precursor metabolites and energy
A0008218biological_processbioluminescence
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 501
ChainResidue
AASP432
AASP434
AASP436
AGLN438
AGLU443
AHOH658

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 502
ChainResidue
ATHR329
AGLU334
AHOH707
AASP323
AASP325
AASP327

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 503
ChainResidue
AASP359
AASP361
AASP363
ATHR365
AGLU370
AHOH641

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 504
ChainResidue
AASP396
AASP398
AASN400
ATYR402
AGLU407
AHOH686

site_idAC5
Number of Residues7
Detailsbinding site for residue CA A 505
ChainResidue
AASP361
AASP363
AASP367
AHOH605
AHOH641
AHOH758
AHOH889

site_idAC6
Number of Residues3
Detailsbinding site for residue FMT A 506
ChainResidue
AHIS112
AGLY141
AHOH739

site_idAC7
Number of Residues3
Detailsbinding site for residue FMT A 507
ChainResidue
AARG267
AARG280
AGLU282

site_idAC8
Number of Residues4
Detailsbinding site for residue FMT A 508
ChainResidue
ALYS265
AARG267
AGLU282
ALYS284

site_idAC9
Number of Residues4
Detailsbinding site for residue FMT A 509
ChainResidue
AGLU175
AASP177
AILE281
AHOH654

site_idAD1
Number of Residues7
Detailsbinding site for residue FMT A 510
ChainResidue
AGLU163
AALA195
ASER230
ATYR232
ALYS237
AHOH612
AHOH616

site_idAD2
Number of Residues3
Detailsbinding site for residue FMT A 511
ChainResidue
AASP363
AFMT512
AHOH758

site_idAD3
Number of Residues7
Detailsbinding site for residue FMT A 512
ChainResidue
ATYR93
AASP327
ATHR329
AFMT511
AHOH638
AHOH646
AHOH866

site_idAD4
Number of Residues3
Detailsbinding site for residue FMT A 513
ChainResidue
AHIS183
AHOH694
AHOH729

site_idAD5
Number of Residues1
Detailsbinding site for residue FMT A 514
ChainResidue
AGLN70

site_idAD6
Number of Residues3
Detailsbinding site for residue FMT A 515
ChainResidue
AVAL159
ASER160
AGLN238

site_idAD7
Number of Residues5
Detailsbinding site for residue FMT A 516
ChainResidue
ALEU60
ALYS79
AHOH613
AHOH646
AHOH660

site_idAD8
Number of Residues6
Detailsbinding site for residue FMT A 517
ChainResidue
AGLU126
ALYS127
AARG128
AHIS130
AHOH648
AHOH927

site_idAD9
Number of Residues4
Detailsbinding site for residue FMT A 518
ChainResidue
AGLN344
AGLU390
AHOH715
AHOH740

site_idAE1
Number of Residues5
Detailsbinding site for residue FMT A 519
ChainResidue
APRO109
AASP110
AARG231
AHOH606
AHOH672

site_idAE2
Number of Residues6
Detailsbinding site for residue EDO A 520
ChainResidue
AHIS80
AARG81
AARG377
ATYR381
AHOH760
AHOH761

site_idAE3
Number of Residues5
Detailsbinding site for residue EDO A 521
ChainResidue
AHOH620
AARG52
AASP383
AILE388
AMET448

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO A 522
ChainResidue
ATYR95
AGLU253
AHOH626
AHOH673

site_idAE5
Number of Residues2
Detailsbinding site for residue EDO A 523
ChainResidue
AHOH647
AHOH847

site_idAE6
Number of Residues7
Detailsbinding site for residue EDO A 524
ChainResidue
ALYS79
AARG81
ALEU91
ASER384
AGLU386
AGLU387
AHOH655

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP325-THR337
AASP361-THR373
AASP398-HIS410
AASP434-GLN446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
AVAL226

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
APIA224
ALEU227

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PDB entries from 2024-07-24

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