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1MCX

STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0001891cellular_componentphagocytic cup
A0002250biological_processadaptive immune response
A0002548biological_processmonocyte chemotaxis
A0002685biological_processregulation of leukocyte migration
A0004859molecular_functionphospholipase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006909biological_processphagocytosis
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A0008360biological_processregulation of cell shape
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030036biological_processactin cytoskeleton organization
A0030659cellular_componentcytoplasmic vesicle membrane
A0031514cellular_componentmotile cilium
A0031901cellular_componentearly endosome membrane
A0032652biological_processregulation of interleukin-1 production
A0032743biological_processpositive regulation of interleukin-2 production
A0042102biological_processpositive regulation of T cell proliferation
A0042119biological_processneutrophil activation
A0045087biological_processinnate immune response
A0045627biological_processpositive regulation of T-helper 1 cell differentiation
A0045629biological_processnegative regulation of T-helper 2 cell differentiation
A0045920biological_processnegative regulation of exocytosis
A0046872molecular_functionmetal ion binding
A0046883biological_processregulation of hormone secretion
A0050727biological_processregulation of inflammatory response
A0070062cellular_componentextracellular exosome
A0071385biological_processcellular response to glucocorticoid stimulus
A0071621biological_processgranulocyte chemotaxis
A0090303biological_processpositive regulation of wound healing
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 347
ChainResidue
AGLY59
AVAL60
AGLU62
AHOH355
AHOH356
AHOH656
AHOH657

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 348
ChainResidue
AGLU105
AASP196
AHOH357
AHOH358
AHOH658
ALYS97
ALEU100

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 349
ChainResidue
AMET127
AGLY129
AGLY131
AASP171
AHOH359
AHOH404

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 350
ChainResidue
ATHR132
AGLU134
AHOH360
AHOH361
AHOH362
AHOH385
AHOH560

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 351
ChainResidue
AGLY210
AARG213
AGLY215
AGLU255
AHOH363
AHOH644

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 352
ChainResidue
AMET286
AGLY288
AGLY290
AGLU330
AHOH364
AHOH365

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 353
ChainResidue
ALEU328
ATHR331
AGLU336
AHOH366
AHOH367
AHOH492
AHOH531

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 354
ChainResidue
AASP253
ALEU256
AGLU261
AHOH368
AHOH588
AHOH660

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdeatiieiLtkRtnaQrqQikaaYlqekgkpLdeaLkkaltGhleevAlaL
ChainResidueDetails
AGLY59-LEU111
AGLY131-LEU183
AGLY215-VAL267
AGLY290-LEU342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBINDING: BINDING => ECO:0007744|PDB:1MCX
ChainResidueDetails
AGLY59
ATHR132
AGLU134
AASP171
AGLY210
AARG213
AGLY215
AASP253
AGLU255
ALEU256
AGLU261
AVAL60
AMET286
AGLY288
AGLY290
ALEU328
AGLU330
ATHR331
AGLU336
AGLU62
ALYS97
ALEU100
AGLU105
AMET127
AGLY129
AGLY131

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by CTSG => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ALYS26

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by TRPM7 => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ASER5

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:3020049
ChainResidueDetails
ATYR21

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ASER34
ASER37

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ATHR41
ATHR136

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10107
ChainResidueDetails
ALYS58

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ALYS239
ALYS312

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250
ChainResidueDetails
AGLN19

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ALYS332

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ALYS214

site_idSWS_FT_FI13
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P10107
ChainResidueDetails
ALYS257

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PDB entries from 2024-08-21

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