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2I94

NMR Structure of recoverin bound to rhodopsin kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001750cellular_componentphotoreceptor outer segment
A0001917cellular_componentphotoreceptor inner segment
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0007601biological_processvisual perception
A0007602biological_processphototransduction
A0016020cellular_componentmembrane
A0042995cellular_componentcell projection
A0043204cellular_componentperikaryon
A0046872molecular_functionmetal ion binding
A0051924biological_processregulation of calcium ion transport
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
APHE73
AASP74
AASN76
AASP78
ATHR80
AGLU85

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AGLY115
ATHR116
AGLU121
AASP110
AASP112
AASN114

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DANSDGTLDfkEY
ChainResidueDetails
AASP74-TYR86
AASP110-VAL122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18339619
ChainResidueDetails
BSER5
AASN76
AASP78
ATHR80
AGLU85

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18339619
ChainResidueDetails
BTHR8

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and autocatalysis => ECO:0000305|PubMed:1527025, ECO:0000305|PubMed:18339619
ChainResidueDetails
BSER21

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9
ChainResidueDetails
AASN114

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0000269|PubMed:8242744, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:1REC, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8, ECO:0007744|PDB:4YI9
ChainResidueDetails
ATHR116

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:17015448, ECO:0000269|PubMed:17020884, ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:26584024, ECO:0000269|PubMed:7630423, ECO:0007744|PDB:1OMR, ECO:0007744|PDB:1OMV, ECO:0007744|PDB:2HET, ECO:0007744|PDB:2I94, ECO:0007744|PDB:4M2O, ECO:0007744|PDB:4M2P, ECO:0007744|PDB:4M2Q, ECO:0007744|PDB:4MLW, ECO:0007744|PDB:4YI8
ChainResidueDetails
AGLU121

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Interaction with GRK1 => ECO:0000269|PubMed:21299498
ChainResidueDetails
ALYS192

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:24189072, ECO:0000269|PubMed:25772009
ChainResidueDetails
ACYS39

site_idSWS_FT_FI9
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:11980481, ECO:0000269|PubMed:1386601, ECO:0000269|PubMed:7630423
ChainResidueDetails
AGLY2

219140

PDB entries from 2024-05-01

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